Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T75498 | Target Info | |||
| Target Name | Quinone reductase 2 (NQO2) | ||||
| Synonyms | Quinone oxidoreductase 2; Qui reductase 2; QR2; NRH:quinone oxidoreductase 2; NRH:qui oxidoreductase 2; NQO2; NAD(P)H qui oxidoreductase 2 | ||||
| Target Type | Successful Target | ||||
| Gene Name | NQO2 | ||||
| Biochemical Class | Diphenol donor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Flavin-Adenine Dinucleotide | Ligand Info | |||
| Canonical SMILES | CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=NC6=C(N=CN=C65)N)O)O)O)O)O | ||||
| InChI | 1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1 | ||||
| InChIKey | VWWQXMAJTJZDQX-UYBVJOGSSA-N | ||||
| PubChem Compound ID | 643975 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4QOG Crystal structure of fad quinone reductase 2 in complex with melatonin at 1.4A | ||||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | Yes | [1] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
|
HIS11
2.830
LYS15
3.482
SER16
3.324
PHE17
3.103
ASN18
2.909
SER20
2.717
PRO102
3.506
LEU103
2.770
TYR104
3.417
TRP105
2.868
PHE106
2.827
|
|||||
| PDB ID: 4QOE The value 'crystal structure of fad quinone reductase 2 at 1.45A | ||||||
| Method | X-ray diffraction | Resolution | 1.45 Å | Mutation | Yes | [2] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFGQ
|
|||||
|
|
HIS11
2.813
LYS15
3.518
SER16
3.215
PHE17
3.042
ASN18
2.883
SER20
2.683
PRO102
3.509
LEU103
2.740
TYR104
3.549
TRP105
2.891
PHE106
2.925
THR147
2.631
|
|||||
| PDB ID: 2QWX Crystal Structure of Quinone Reductase II | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [3] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
|
HIS11
2.793
LYS15
3.644
SER16
3.305
PHE17
2.891
ASN18
2.864
SER20
2.505
PRO102
3.530
LEU103
2.800
TYR104
3.385
TRP105
2.815
PHE106
2.742
THR147
2.601
|
|||||
| PDB ID: 4XDG Crystal Structure of Quinone Reductase II in complex with 2-(4-aminophenyl)-5-methoxy-1-oxy-indol-3-one molecule | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [4] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFGQ
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.733
LYS15
3.254
SER16
3.213
PHE17
3.166
ASN18
2.882
SER20
2.741
PRO102
3.481
LEU103
2.715
TYR104
3.425
TRP105
2.837
PHE106
2.864
THR147
2.677
|
|||||
| PDB ID: 4QOH Crystal structure of fad quinone reductase 2 in complex with resveratrol at 1.6A | ||||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | Yes | [5] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFGQ
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.792
LYS15
3.558
SER16
3.180
PHE17
2.985
ASN18
2.861
SER20
2.835
PRO102
3.538
LEU103
2.751
TYR104
3.385
TRP105
2.881
PHE106
2.901
THR147
2.618
|
|||||
| PDB ID: 3OX3 X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [6] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.780
LYS15
3.353
SER16
3.126
PHE17
3.022
ASN18
2.913
SER20
2.614
PRO102
3.580
LEU103
2.720
TYR104
3.392
TRP105
2.852
PHE106
2.971
THR147
2.672
|
|||||
| PDB ID: 3G5M Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory activity | ||||||
| Method | X-ray diffraction | Resolution | 1.84 Å | Mutation | No | [7] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.733
LYS15
3.334
SER16
3.042
PHE17
3.031
ASN18
2.889
SER20
2.573
PRO102
3.339
LEU103
2.749
TYR104
3.474
TRP105
2.869
PHE106
2.908
THR147
2.582
|
|||||
| PDB ID: 3OWX X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 1.85 Å | Mutation | No | [6] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.678
LYS15
3.329
SER16
3.228
PHE17
3.119
ASN18
2.905
SER20
2.627
PRO102
3.441
LEU103
2.800
TYR104
3.433
TRP105
2.822
PHE106
2.959
THR147
2.761
|
|||||
| PDB ID: 4XDH Crystal Structure of Quinone Reductase II in complex with a 2-(4-methoxy-phenyl)-5-methoxy-indol-3-one molecule | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [4] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFGQ
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.798
LYS15
3.425
SER16
3.231
PHE17
3.129
ASN18
2.857
SER20
2.695
PRO102
3.466
LEU103
2.773
TYR104
3.472
TRP105
2.864
PHE106
2.859
THR147
2.681
|
|||||
| PDB ID: 3GAM Synthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory activity | ||||||
| Method | X-ray diffraction | Resolution | 1.98 Å | Mutation | No | [7] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.716
LYS15
2.932
SER16
3.283
PHE17
3.151
ASN18
2.681
SER20
2.484
PRO102
3.231
LEU103
2.834
TYR104
3.370
TRP105
2.775
PHE106
2.856
THR147
2.674
|
|||||
| PDB ID: 3OX1 X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.696
LYS15
3.386
SER16
3.114
PHE17
3.113
ASN18
2.873
SER20
2.683
PRO102
3.381
LEU103
2.838
TYR104
3.435
TRP105
2.854
PHE106
2.898
THR147
2.698
|
|||||
| PDB ID: 3OVM X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 2.09 Å | Mutation | No | [6] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.729
LYS15
3.111
SER16
3.199
PHE17
3.252
ASN18
2.880
SER20
2.735
PRO102
3.281
LEU103
2.803
TYR104
3.454
TRP105
2.875
PHE106
2.943
|
|||||
| PDB ID: 1ZX1 Human quinone oxidoreductase 2 (NQO2) in complex with the cytostatic prodrug CB1954 | ||||||
| Method | X-ray diffraction | Resolution | 2.16 Å | Mutation | No | [8] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.755
LYS15
3.323
SER16
2.956
PHE17
3.264
ASN18
2.814
SER20
2.639
PRO102
3.449
LEU103
2.742
TYR104
3.397
TRP105
2.765
PHE106
2.906
THR147
2.628
|
|||||
| PDB ID: 3OWH X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 2.28 Å | Mutation | No | [6] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.749
LYS15
3.259
SER16
3.254
PHE17
3.159
ASN18
2.770
SER20
2.575
PRO102
3.492
LEU103
2.697
TYR104
3.433
TRP105
2.834
PHE106
2.969
|
|||||
| PDB ID: 3OX2 X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values | ||||||
| Method | X-ray diffraction | Resolution | 2.41 Å | Mutation | No | [6] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.619
LYS15
3.225
SER16
3.241
PHE17
3.210
ASN18
2.807
SER20
2.644
PRO102
3.699
LEU103
2.849
TYR104
3.429
TRP105
2.847
PHE106
2.917
THR147
2.764
|
|||||
| PDB ID: 4U7H Oxidized quinone reductase 2 in complex with CK2 inhibitor DMAT | ||||||
| Method | X-ray diffraction | Resolution | 1.48 Å | Mutation | Yes | [9] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.905
LYS15
3.670
SER16
2.616
PHE17
2.455
ASN18
1.950
GLY19
4.646
SER20
2.050
PRO102
3.081
LEU103
2.660
TYR104
2.567
TRP105
2.043
PHE106
2.178
SER107
4.728
|
|||||
| PDB ID: 1SG0 Crystal structure analysis of QR2 in complex with resveratrol | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [10] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
3.252
LYS15
3.542
SER16
3.039
PHE17
3.053
ASN18
3.270
SER20
2.710
PRO102
3.767
LEU103
3.041
TYR104
3.389
TRP105
2.767
PHE106
2.831
THR147
3.097
|
|||||
| PDB ID: 1XI2 Quinone Reductase 2 in Complex with Cancer Prodrug CB1954 | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [11] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
3.137
LYS15
3.313
SER16
3.089
PHE17
2.891
ASN18
2.929
SER20
2.762
PRO102
3.372
LEU103
2.853
TYR104
3.430
TRP105
2.789
PHE106
2.873
|
|||||
| PDB ID: 3UXE Design, Synthesis and Biological Evaluation of Potent Quinoline and Pyrroloquinoline Ammosamide Analogues as Inhibitors for Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | Yes | [12] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:198 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.773
LYS15
3.535
SER16
3.231
PHE17
3.172
ASN18
2.820
SER20
2.817
PRO102
3.440
LEU103
2.729
TYR104
3.371
TRP105
2.822
PHE106
2.815
THR147
2.688
|
|||||
| PDB ID: 3UXH Design, Synthesis and Biological Evaluation of Potetent Quinoline and Pyrroloquinoline Ammosamide Analogues as Inhibitors of Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.53 Å | Mutation | Yes | [12] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.775
LYS15
3.231
SER16
2.941
PHE17
2.824
ASN18
2.793
SER20
2.646
PRO102
3.446
LEU103
2.654
TYR104
3.360
TRP105
2.836
PHE106
2.773
THR147
2.696
|
|||||
| PDB ID: 3NFR Casimiroin analog inhibitor of quinone reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.57 Å | Mutation | No | [13] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.751
LYS15
3.176
SER16
3.236
PHE17
2.813
ASN18
2.947
SER20
2.454
PRO102
3.434
LEU103
2.698
TYR104
3.352
TRP105
2.716
PHE106
2.786
|
|||||
| PDB ID: 3NHL X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.57 Å | Mutation | No | [14] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.809
LYS15
3.175
SER16
3.018
PHE17
3.028
ASN18
2.878
SER20
2.484
PRO102
3.449
LEU103
2.710
TYR104
3.300
TRP105
2.750
PHE106
2.678
THR147
2.510
|
|||||
| PDB ID: 2QX8 Crystal Structure of Quinone Reductase II | ||||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [3] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.886
LYS15
3.439
SER16
3.431
PHE17
2.748
ASN18
2.812
SER20
2.550
PRO102
3.508
LEU103
2.652
TYR104
3.299
TRP105
2.752
PHE106
2.738
THR147
2.637
|
|||||
| PDB ID: 3O2N X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [15] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.670
LYS15
3.146
SER16
2.922
PHE17
3.003
ASN18
2.891
SER20
2.522
PRO102
3.416
LEU103
2.685
TYR104
3.362
TRP105
2.806
PHE106
2.747
THR147
2.645
|
|||||
| PDB ID: 2QX4 Crystal Structure of Quinone Reductase II | ||||||
| Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | No | [3] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.776
LYS15
3.673
SER16
3.434
PHE17
2.933
ASN18
2.878
SER20
2.523
PRO102
3.661
LEU103
2.772
TYR104
3.473
TRP105
2.848
PHE106
2.684
THR147
2.555
|
|||||
| PDB ID: 3NHW X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | No | [16] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.789
LYS15
3.113
SER16
3.147
PHE17
3.012
ASN18
2.842
SER20
2.524
PRO102
3.426
LEU103
2.691
TYR104
3.404
TRP105
2.845
PHE106
2.814
THR147
2.724
|
|||||
| PDB ID: 3NHP X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [17] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.748
LYS15
3.216
SER16
3.258
PHE17
2.907
ASN18
2.834
SER20
2.450
PRO102
3.460
LEU103
2.696
TYR104
3.345
TRP105
2.669
PHE106
2.795
|
|||||
| PDB ID: 2QX6 Crystal Structure of Quinone Reductase II | ||||||
| Method | X-ray diffraction | Resolution | 1.75 Å | Mutation | No | [3] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.769
LYS15
3.629
SER16
3.299
PHE17
2.874
ASN18
2.746
SER20
2.537
PRO102
3.560
LEU103
2.666
TYR104
3.449
TRP105
2.759
PHE106
2.677
THR147
2.512
|
|||||
| PDB ID: 3NHS X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.78 Å | Mutation | No | [18] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.550
LYS15
3.002
SER16
3.207
PHE17
3.250
ASN18
2.886
SER20
2.645
PRO102
3.478
LEU103
2.754
TYR104
3.408
TRP105
2.871
PHE106
2.940
THR147
2.690
|
|||||
| PDB ID: 3NHR X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [19] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFGQ
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.668
LYS15
3.023
SER16
3.064
PHE17
2.966
ASN18
2.852
SER20
2.542
PRO102
3.550
LEU103
2.715
TYR104
3.432
TRP105
2.881
PHE106
2.795
THR147
2.665
|
|||||
| PDB ID: 4U7F Reduced quinone reductase 2 in complex with CK2 inhibitor DMAT | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | Yes | [9] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.882
LYS15
3.720
SER16
3.205
PHE17
2.424
ASN18
2.077
GLY19
4.719
SER20
2.750
PRO102
3.449
LEU103
2.771
TYR104
3.595
TRP105
2.066
PHE106
2.382
|
|||||
| PDB ID: 4ZVK Reduced quinone reductase 2 in complex with ethidium | ||||||
| Method | X-ray diffraction | Resolution | 1.87 Å | Mutation | No | [20] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.901
LYS15
3.578
SER16
2.578
PHE17
2.191
ASN18
1.991
GLY19
4.633
SER20
2.083
PRO102
3.116
LEU103
2.747
TYR104
2.675
TRP105
2.041
PHE106
2.348
SER107
4.954
|
|||||
| PDB ID: 4ZVN Reduced quinone reductase 2 in complex with acridine orange | ||||||
| Method | X-ray diffraction | Resolution | 1.87 Å | Mutation | No | [20] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.971
LYS15
3.648
SER16
3.218
PHE17
2.277
ASN18
2.103
GLY19
4.612
SER20
2.888
PRO102
3.523
LEU103
2.727
TYR104
3.556
TRP105
1.989
PHE106
2.359
|
|||||
| PDB ID: 5BUC Oxidized quinone reductase 2 in complex with ethidium | ||||||
| Method | X-ray diffraction | Resolution | 1.87 Å | Mutation | No | [21] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.773
LYS15
3.607
SER16
3.128
PHE17
2.201
ASN18
1.921
GLY19
4.610
SER20
2.751
PRO102
3.564
LEU103
2.692
TYR104
3.435
TRP105
2.083
PHE106
2.251
SER107
4.812
|
|||||
| PDB ID: 3NHU X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [22] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.793
LYS15
3.185
SER16
3.219
PHE17
3.217
ASN18
2.850
SER20
2.734
PRO102
3.342
LEU103
2.727
TYR104
3.496
TRP105
2.891
PHE106
2.892
THR147
2.607
|
|||||
| PDB ID: 3NHY X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [23] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.717
LYS15
3.259
SER16
3.086
PHE17
3.065
ASN18
2.825
SER20
2.650
PRO102
3.384
LEU103
2.747
TYR104
3.430
TRP105
2.819
PHE106
2.920
THR147
2.695
|
|||||
| PDB ID: 4ZVL Oxidized quinone reductase 2 in complex with acridine orange | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [20] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.879
LYS15
3.376
SER16
2.534
PHE17
2.368
ASN18
2.000
GLY19
4.639
SER20
2.650
PRO102
3.034
LEU103
2.663
TYR104
2.617
TRP105
2.055
PHE106
2.237
SER107
4.811
|
|||||
| PDB ID: 4GQI Synthesis of novel MT3 receptor ligands via unusual Knoevenagel condensation | ||||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | No | [24] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.662
LYS15
3.363
SER16
3.135
PHE17
2.932
ASN18
2.812
SER20
2.760
PRO102
3.463
LEU103
2.710
TYR104
3.409
TRP105
2.813
PHE106
2.893
THR147
2.755
|
|||||
| PDB ID: 3NHK X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.96 Å | Mutation | No | [25] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.798
LYS15
3.339
SER16
3.070
PHE17
3.225
ASN18
2.899
SER20
2.771
PRO102
3.436
LEU103
2.720
TYR104
3.356
TRP105
2.822
PHE106
2.810
THR147
2.593
|
|||||
| PDB ID: 4U7G Oxidized quinone reductase 2 in complex with CK2 inhibitor TBBz | ||||||
| Method | X-ray diffraction | Resolution | 1.96 Å | Mutation | Yes | [9] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.786
LYS15
3.394
SER16
3.159
PHE17
2.369
ASN18
1.925
GLY19
4.758
SER20
2.119
PRO102
3.451
LEU103
2.738
TYR104
3.408
TRP105
2.134
PHE106
2.264
SER107
4.777
|
|||||
| PDB ID: 4ZVM Oxidized quinone reductase 2 in complex with doxorubicin | ||||||
| Method | X-ray diffraction | Resolution | 1.97 Å | Mutation | No | [20] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.007
LYS15
3.730
SER16
2.666
PHE17
2.354
ASN18
2.077
GLY19
4.685
SER20
2.054
PRO102
2.943
LEU103
2.780
TYR104
2.631
TRP105
2.196
PHE106
2.275
SER107
4.752
|
|||||
| PDB ID: 3NHF X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [26] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.717
LYS15
3.184
SER16
3.131
PHE17
3.145
ASN18
2.786
SER20
2.609
PRO102
3.413
LEU103
2.738
TYR104
3.432
TRP105
2.821
PHE106
2.926
THR147
2.782
|
|||||
| PDB ID: 1QR2 HUMAN QUINONE REDUCTASE TYPE 2 | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [27] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.830
LYS15
3.528
SER16
3.234
PHE17
1.820
ASN18
1.803
GLY19
4.705
SER20
2.561
PRO102
3.192
LEU103
2.672
TYR104
3.308
TRP105
1.838
PHE106
1.864
SER107
4.451
|
|||||
| PDB ID: 2QMZ Quinone Reductase 2 in Complex with Dopamine | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [28] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.891
LYS15
3.340
SER16
3.232
PHE17
3.003
ASN18
2.812
SER20
2.724
PRO102
3.317
LEU103
2.687
TYR104
3.344
TRP105
2.672
PHE106
2.817
|
|||||
| PDB ID: 3TZB Quinone Oxidoreductase (NQ02) bound to NSC13000 | ||||||
| Method | X-ray diffraction | Resolution | 2.19 Å | Mutation | No | [29] |
| PDB Sequence |
AMGKKVLIVY
9 AHQEPKSFNG19 SLKNVAVDEL29 SRQGCTVTVS39 DLYAMNFEPR49 ATDKDITGTL 59 SNPEVFNYGV69 ETHEAYKQRS79 LASDITDEQK89 KVREADLVIF99 QFPLYWFSVP 109 AILKGWMDRV119 LCQGFAFDIP129 GFYDSGLLQG139 KLALLSVTTG149 GTAEMYTKTG 159 VNGDSRYFLW169 PLQHGTLHFC179 GFKVLAPQIS189 FAPEIASEEE199 RKGMVAAWSQ 209 RLQTIWKEEP219 IPCTAHWHFG229
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.757
LYS15
3.462
SER16
3.158
PHE17
3.071
ASN18
2.807
SER20
2.539
PRO102
3.487
LEU103
2.720
TYR104
3.439
TRP105
2.821
PHE106
2.706
THR147
2.648
|
|||||
| PDB ID: 4GR9 Synthesis of novel MT3 receptor ligands via unusual Knoevenagel condensation | ||||||
| Method | X-ray diffraction | Resolution | 2.29 Å | Mutation | No | [24] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.686
LYS15
3.455
SER16
3.199
PHE17
3.098
ASN18
2.808
SER20
2.713
PRO102
3.475
LEU103
2.813
TYR104
3.387
TRP105
2.902
PHE106
2.815
THR147
2.740
|
|||||
| PDB ID: 2QX9 Crystal Structure of Quinone Reductase II | ||||||
| Method | X-ray diffraction | Resolution | 2.31 Å | Mutation | No | [3] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.914
LYS15
3.152
SER16
3.250
PHE17
3.075
ASN18
2.649
SER20
2.710
PRO102
3.915
LEU103
3.002
TYR104
3.407
TRP105
2.830
PHE106
2.927
|
|||||
| PDB ID: 3NHJ X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 2.33 Å | Mutation | No | [30] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.481
LYS15
3.120
SER16
3.173
PHE17
3.243
ASN18
2.704
SER20
2.534
PRO102
3.563
LEU103
2.949
TYR104
3.448
TRP105
2.791
PHE106
2.880
THR147
2.873
|
|||||
| PDB ID: 2QR2 HUMAN QUINONE REDUCTASE TYPE 2, COMPLEX WITH MENADIONE | ||||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [27] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.045
LYS15
3.054
SER16
3.193
PHE17
2.183
ASN18
1.937
GLY19
4.697
SER20
1.954
PRO102
3.471
LEU103
2.723
TYR104
3.442
TRP105
1.947
PHE106
1.891
SER107
4.407
|
|||||
| PDB ID: 2QMY Quinone Reductase 2 in complex with adrenochrome | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [31] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.784
LYS15
3.452
SER16
3.150
PHE17
2.639
ASN18
2.885
SER20
2.695
PRO102
3.338
LEU103
2.875
TYR104
3.395
TRP105
2.876
PHE106
2.882
THR147
2.888
|
|||||
| PDB ID: 4FGL Reduced quinone reductase 2 in complex with chloroquine | ||||||
| Method | X-ray diffraction | Resolution | 1.20 Å | Mutation | No | [32] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:198 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.902
LYS15
2.415
SER16
2.459
PHE17
2.217
ASN18
1.958
GLY19
4.726
SER20
2.385
PRO102
2.417
LEU103
1.812
TYR104
2.643
TRP105
2.074
PHE106
2.205
SER107
4.840
|
|||||
| PDB ID: 4FGJ Oxidized quinone reductase 2 in complex with primaquine | ||||||
| Method | X-ray diffraction | Resolution | 1.35 Å | Mutation | No | [33] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:12 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:101 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:191 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.933
GLN12
4.934
LYS15
2.863
SER16
2.511
PHE17
2.312
ASN18
1.976
GLY19
4.665
SER20
2.266
PHE101
4.884
PRO102
2.418
LEU103
1.894
TYR104
2.543
TRP105
2.048
PHE106
2.231
|
|||||
| PDB ID: 4FGK Oxidized quinone reductase 2 in complex with chloroquine | ||||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | No | [34] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:191 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.851
LYS15
2.812
SER16
2.482
PHE17
2.275
ASN18
2.009
GLY19
4.662
SER20
1.823
PRO102
2.451
LEU103
1.881
TYR104
2.552
TRP105
2.039
PHE106
2.216
SER107
4.818
|
|||||
| PDB ID: 3FW1 Quinone Reductase 2 | ||||||
| Method | X-ray diffraction | Resolution | 1.75 Å | Mutation | No | [35] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:12 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:191 or .A:192 or .A:193 or .A:196 or .A:197 or .A:198 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.008
GLN12
4.806
LYS15
2.146
SER16
2.543
PHE17
2.103
ASN18
1.945
GLY19
4.747
SER20
2.711
PRO102
2.203
LEU103
2.457
TYR104
2.502
TRP105
2.055
PHE106
2.197
SER107
4.750
THR147
2.604
|
|||||
| PDB ID: 3TEM Quinone Oxidoreductase (NQ02) bound to the imidazoacridin-6-one 6a1 | ||||||
| Method | X-ray diffraction | Resolution | 1.45 Å | Mutation | No | [36] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
1.994
LYS15
3.541
SER16
2.509
PHE17
2.252
ASN18
2.011
GLY19
4.653
SER20
1.995
PRO102
3.096
LEU103
2.651
TYR104
2.493
TRP105
1.996
PHE106
2.054
SER107
4.705
|
|||||
| PDB ID: 3TE7 Quinone Oxidoreductase (NQ02) bound to the imidazoacridin-6-one 5a1 | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [36] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNFEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.804
LYS15
3.499
SER16
3.175
PHE17
3.015
ASN18
2.869
SER20
2.741
PRO102
3.512
LEU103
2.841
TYR104
3.395
TRP105
2.785
PHE106
2.783
THR147
2.643
|
|||||
| PDB ID: 2BZS Binding of anti-cancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex. | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [37] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:66 or .A:67 or .A:68 or .A:117; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| PDB ID: 5LBY Structure of the human quinone reductase 2 (NQO2) in complex with crenolanib | ||||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | No | [38] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNLEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.832
LYS15
3.362
SER16
3.212
PHE17
2.890
ASN18
2.855
SER20
2.652
PRO102
3.551
LEU103
2.823
TYR104
3.346
TRP105
2.874
PHE106
2.852
THR147
2.652
|
|||||
| PDB ID: 5LBZ Structure of the human quinone reductase 2 (NQO2) in complex with pacritinib | ||||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | No | [38] |
| PDB Sequence |
KKVLIVYAHQ
12 EPKSFNGSLK22 NVAVDELSRQ32 GCTVTVSDLY42 AMNLEPRATD52 KDITGTLSNP 62 EVFNYGVETH72 EAYKQRSLAS82 DITDEQKKVR92 EADLVIFQFP102 LYWFSVPAIL 112 KGWMDRVLCQ122 GFAFDIPGFY132 DSGLLQGKLA142 LLSVTTGGTA152 EMYTKTGVNG 162 DSRYFLWPLQ172 HGTLHFCGFK182 VLAPQISFAP192 EIASEEERKG202 MVAAWSQRLQ 212 TIWKEEPIPC222 TAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.806
LYS15
3.297
SER16
3.262
PHE17
2.861
ASN18
2.878
SER20
2.603
PRO102
3.510
LEU103
2.778
TYR104
3.378
TRP105
2.875
PHE106
2.854
|
|||||
| PDB ID: 5LBU Structure of the human quinone reductase 2 (NQO2) in complex with to CL097 | ||||||
| Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | No | [39] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNLEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.882
LYS15
3.606
SER16
3.137
PHE17
2.978
ASN18
2.878
SER20
2.733
PRO102
3.422
LEU103
2.723
TYR104
3.444
TRP105
2.856
PHE106
2.968
|
|||||
| PDB ID: 5LBT Structure of the human quinone reductase 2 (NQO2) in complex with imiquimod | ||||||
| Method | X-ray diffraction | Resolution | 1.75 Å | Mutation | No | [40] |
| PDB Sequence |
GKKVLIVYAH
11 QEPKSFNGSL21 KNVAVDELSR31 QGCTVTVSDL41 YAMNLEPRAT51 DKDITGTLSN 61 PEVFNYGVET71 HEAYKQRSLA81 SDITDEQKKV91 READLVIFQF101 PLYWFSVPAI 111 LKGWMDRVLC121 QGFAFDIPGF131 YDSGLLQGKL141 ALLSVTTGGT151 AEMYTKTGVN 161 GDSRYFLWPL171 QHGTLHFCGF181 KVLAPQISFA191 PEIASEEERK201 GMVAAWSQRL 211 QTIWKEEPIP221 CTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.799
LYS15
3.556
SER16
3.191
PHE17
3.069
ASN18
2.893
SER20
2.734
PRO102
3.528
LEU103
2.702
TYR104
3.459
TRP105
2.876
PHE106
2.914
THR147
2.658
|
|||||
| PDB ID: 5LBW Structure of the human quinone reductase 2 (NQO2) in complex with volitinib | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [38] |
| PDB Sequence |
KKVLIVYAHQ
12 EPKSFNGSLK22 NVAVDELSRQ32 GCTVTVSDLY42 AMNLEPRATD52 KDITGTLSNP 62 EVFNYGVETH72 EAYKQRSLAS82 DITDEQKKVR92 EADLVIFQFP102 LYWFSVPAIL 112 KGWMDRVLCQ122 GFAFDIPGFY132 DSGLLQGKLA142 LLSVTTGGTA152 EMYTKTGVNG 162 DSRYFLWPLQ172 HGTLHFCGFK182 VLAPQISFAP192 EIASEEERKG202 MVAAWSQRLQ 212 TIWKEEPIPC222 TAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.750
LYS15
3.495
SER16
3.277
PHE17
3.150
ASN18
2.680
SER20
2.584
PRO102
3.212
LEU103
2.899
TYR104
3.491
TRP105
2.858
PHE106
2.881
THR147
2.543
|
|||||
| PDB ID: 3O73 Crystal structure of quinone reductase 2 in complex with the indolequinone MAC627 | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [41] |
| PDB Sequence |
AGKKVLIVYA
10 HQEPKSFNGS20 LKNVAVDELS30 RQGCTVTVSD40 LYAMNFEPRA50 TDKDITGTLS 60 NPEVFNYGVE70 THEAYKQRSL80 ASDITDEQKK90 VREADLVIFQ100 FPLYWFSVPA 110 ILKGWMDRVL120 CQGFAFDIPG130 FYDSGLLQGK140 LALLSVTTGG150 TAEMYTKTGV 160 NGDSRYFLWP170 LQHGTLHFCG180 FKVLAPQISF190 APEIASEEER200 KGMVAAWSQR 210 LQTIWKEEPI220 PCTAHWHFGQ230
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:11 or .A:15 or .A:16 or .A:17 or .A:18 or .A:20 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:147 or .A:148 or .A:149 or .A:150 or .A:155 or .A:161 or .A:192 or .A:193 or .A:197 or .A:200 or .A:201 or .A:204; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS11
2.597
LYS15
3.264
SER16
3.258
PHE17
3.019
ASN18
2.724
SER20
2.917
PRO102
3.551
LEU103
2.697
TYR104
3.491
TRP105
2.650
PHE106
2.974
THR147
2.633
|
|||||
| PDB ID: 7O4D QR2 inhibitor from a novel sulfanamide series to tackle age related oxidative stress and cognitive decline | ||||||
| Method | X-ray diffraction | Resolution | 2.25 Å | Mutation | Yes | [42] |
| PDB Sequence |
AGKKVLIVYA
11 HQEPKSFNGS21 LKNVAVDELS31 RQGCTVTVSD41 LYAMNFEPRA51 TDKDITGTLS 61 NPEVFNYGVE71 THEAYKQRSL81 ASDITDEQKK91 VREADLVIFQ101 FPLYWFSVPA 111 ILKGWMDRVL121 CQGFAFDIPG131 FYDSGLLQGK141 LALLSVTTGG151 TAEMYTKTGV 161 NGDSRYFLWP171 LQHGTLHFCG181 FKVLAPQISF191 APEIASEEER201 KGMVAAWSQR 211 LQTIWKEEPI221 PCTAHWHFG
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:12 or .A:16 or .A:17 or .A:18 or .A:19 or .A:21 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:148 or .A:149 or .A:150 or .A:151 or .A:156 or .A:193 or .A:194 or .A:198 or .A:201 or .A:202 or .A:205; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS12
2.874
LYS16
3.691
SER17
3.180
PHE18
2.918
ASN19
2.989
SER21
2.937
PRO103
3.381
LEU104
2.674
TYR105
3.427
TRP106
2.839
PHE107
3.008
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal structure of fad quinone reductase 2 in complex with melatonin at 1.4A | ||||
| REF 2 | The value 'crystal structure of fad quinone reductase 2 at 1.45A | ||||
| REF 3 | Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2. Biochem J. 2008 Jul 1;413(1):81-91. | ||||
| REF 4 | Role of Quinone Reductase 2 in the Antimalarial Properties of Indolone-Type Derivatives. Molecules. 2017 Jan 30;22(2):210. | ||||
| REF 5 | Crystal structure of fad quinone reductase 2 in complex | ||||
| REF 6 | X-ray structural studies of quinone reductase 2 nanomolar range inhibitors. Protein Sci. 2011 Jul;20(7):1182-95. | ||||
| REF 7 | Synthesis of casimiroin and optimization of its quinone reductase 2 and aromatase inhibitory activities. J Med Chem. 2009 Apr 9;52(7):1873-84. | ||||
| REF 8 | Human quinone oxidoreductase 2 (NQO2) in complex with the cytostatic prodrug CB1954 | ||||
| REF 9 | Quinone reductase 2 is an adventitious target of protein kinase CK2 inhibitors TBBz (TBI) and DMAT. Biochemistry. 2015 Jan 13;54(1):47-59. | ||||
| REF 10 | Crystal structure of quinone reductase 2 in complex with resveratrol. Biochemistry. 2004 Sep 14;43(36):11417-26. | ||||
| REF 11 | Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954. Biochem Biophys Res Commun. 2005 Oct 14;336(1):332-8. | ||||
| REF 12 | Design, synthesis, and biological evaluation of potent quinoline and pyrroloquinoline ammosamide analogues as inhibitors of quinone reductase 2. J Med Chem. 2012 Jan 12;55(1):367-77. | ||||
| REF 13 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 14 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 15 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 16 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 17 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 18 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 19 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 20 | Binding of DNA-Intercalating Agents to Oxidized and Reduced Quinone Reductase 2. Biochemistry. 2015 Dec 29;54(51):7438-48. | ||||
| REF 21 | Structure of quinone reductase 2 in complex with DNA intercalating agents | ||||
| REF 22 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 23 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 24 | Synthesis of novel MT3 receptor ligands via an unusual Knoevenagel condensation. Bioorg Med Chem Lett. 2012 Dec 15;22(24):7578-81. | ||||
| REF 25 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 26 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 27 | Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry. 1999 Aug 3;38(31):9881-6. | ||||
| REF 28 | Quinone Reductase 2 Regulates Catecholamine Oxidation | ||||
| REF 29 | In silico screening reveals structurally diverse, nanomolar inhibitors of NQO2 that are functionally active in cells and can modulate NF-KappaB signaling. Mol Cancer Ther. 2012 Jan;11(1):194-203. | ||||
| REF 30 | X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its Analogs Bound to Human Quinone Reductase 2 | ||||
| REF 31 | Quinone Reductase 2 regulates Catecholamine oxidation | ||||
| REF 32 | Crystal structures of quinone reductase 2 bound to antimalarial drugs reveal conformational change upon reduction | ||||
| REF 33 | Crystal structures of quinone reductase 2 bound to antimalarial drugs reveal conformational change upon reduction | ||||
| REF 34 | Crystal structures of quinone reductase 2 bound to antimalarial drugs reveal conformational change upon reduction | ||||
| REF 35 | The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2). BMC Struct Biol. 2009 Feb 24;9:7. | ||||
| REF 36 | Novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2): crystal structures, biochemical activity, and intracellular effects of imidazoacridin-6-ones. J Med Chem. 2011 Oct 13;54(19):6597-611. | ||||
| REF 37 | Binding of the anticancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex. J Med Chem. 2005 Dec 1;48(24):7714-9. | ||||
| REF 38 | The target landscape of clinical kinase drugs. Science. 2017 Dec 1;358(6367):eaan4368. | ||||
| REF 39 | Imiquimod Inhibits Mitochondrial Complex I and Induces K+ efflux-independent Nlrp3 Inflammasome Activation via Nek7 | ||||
| REF 40 | Imiquimod Inhibits Mitochondrial Complex I and Induces K+ efflux-independent Nlrp3 Inflammasome Activation via Nek7 | ||||
| REF 41 | Mechanism-based inhibition of quinone reductase 2 (NQO2): selectivity for NQO2 over NQO1 and structural basis for flavoprotein inhibition. Chembiochem. 2011 May 16;12(8):1203-8. | ||||
| REF 42 | A Novel Sulfanamide Series of QR2 Inhibitors to Tackle Age Related Oxidative Stress and Cognitive Decline | ||||
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