Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T30803 | Target Info | |||
| Target Name | Glutathione reductase (GR) | ||||
| Synonyms | Glutathione reductase, mitochondrial; GRase; GRD1; GLUR | ||||
| Target Type | Patented-recorded Target | ||||
| Gene Name | GSR | ||||
| Biochemical Class | Sulfur 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: 2AAQ Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI | ||||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
|
ILE26
4.020
GLY27
3.379
GLY28
3.722
GLY29
3.190
SER30
3.553
GLY31
2.717
GLY32
3.974
VAL49
3.322
GLU50
2.617
SER51
3.397
HIS52
3.845
LYS53
3.403
GLY55
3.921
GLY56
2.875
THR57
3.001
CYS58
3.275
VAL61
3.575
GLY62
3.787
CYS63
3.295
LYS66
2.875
GLY128
3.804
HIS129
3.140
ALA130
3.017
ALA155
3.569
THR156
3.264
GLY157
2.946
GLY158
3.834
SER177
3.625
PHE181
3.627
TYR197
3.813
ILE198
4.082
GLU201
4.490
ARG291
3.311
ASN294
3.872
LEU298
3.793
VAL329
4.779
GLY330
4.027
ASP331
2.868
VAL332
4.644
LEU337
3.520
LEU338
3.373
THR339
2.958
PRO340
2.917
ALA342
3.735
PHE372
4.000
|
|||||
| PDB ID: 3DK9 Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 0.95 Å | Mutation | No | [2] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
|
|||||
|
|
ILE26
3.753
GLY27
3.254
GLY28
4.052
GLY29
3.315
SER30
3.250
GLY31
2.836
GLY32
4.159
VAL49
3.708
GLU50
2.658
SER51
3.174
HIS52
3.794
LYS53
3.666
GLY55
4.134
GLY56
3.214
THR57
2.789
CYS58
3.362
VAL61
3.733
GLY62
3.635
CYS63
3.261
LYS66
2.736
GLY128
3.361
HIS129
3.261
ALA130
3.010
ALA155
3.315
THR156
3.401
GLY157
3.364
GLY158
4.391
SER177
3.808
PHE181
4.248
TYR197
3.109
ILE198
3.981
GLU201
4.621
MET202
3.939
ARG291
3.385
ASN294
3.534
LEU298
3.616
VAL329
4.270
GLY330
3.385
ASP331
2.801
VAL332
4.507
LEU337
3.290
LEU338
3.144
THR339
2.943
PRO340
3.097
ALA342
3.955
PHE372
4.291
|
|||||
| PDB ID: 3DJJ Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 1.10 Å | Mutation | No | [2] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
|
|||||
|
|
ILE26
3.755
GLY27
3.276
GLY28
3.998
GLY29
3.407
SER30
3.179
GLY31
2.886
GLY32
4.241
VAL49
3.725
GLU50
2.682
SER51
3.158
HIS52
3.822
LYS53
3.724
GLY55
4.308
GLY56
3.201
THR57
2.702
CYS58
3.457
VAL61
3.638
GLY62
3.568
CYS63
3.256
LYS66
2.771
GLY128
3.426
HIS129
3.292
ALA130
3.025
ALA155
3.353
THR156
3.378
GLY157
3.376
GLY158
4.191
SER177
3.813
PHE181
4.179
ILE198
3.905
GLU201
4.673
MET202
4.098
ARG291
3.431
ASN294
3.540
LEU298
3.616
VAL329
4.397
GLY330
3.453
ASP331
2.759
VAL332
4.594
LEU337
3.321
LEU338
3.214
THR339
2.966
PRO340
3.160
ALA342
4.107
PHE372
3.613
|
|||||
| PDB ID: 3DK8 Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 1.10 Å | Mutation | No | [2] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
|
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|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:202 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.789
GLY27
3.291
GLY28
3.922
GLY29
3.400
SER30
3.261
GLY31
2.907
GLY32
4.225
VAL49
3.770
GLU50
2.677
SER51
3.151
HIS52
3.759
LYS53
3.761
GLY55
4.368
GLY56
3.240
THR57
2.698
CYS58
3.399
VAL61
3.706
GLY62
3.633
CYS63
3.272
LYS66
2.726
GLY128
3.385
HIS129
3.293
ALA130
2.988
ALA155
3.343
THR156
3.396
GLY157
3.378
GLY158
4.156
SER177
3.919
PHE181
4.208
TYR197
3.117
ILE198
4.016
GLU201
4.480
MET202
3.956
ARG291
3.415
ASN294
3.499
LEU298
3.591
VAL329
4.346
GLY330
3.422
ASP331
2.754
VAL332
4.552
LEU337
3.320
LEU338
3.226
THR339
2.963
PRO340
3.124
ALA342
4.099
PHE372
4.002
|
|||||
| PDB ID: 3DK4 Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 1.20 Å | Mutation | No | [2] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:202 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.827
GLY27
3.292
GLY28
3.993
GLY29
3.380
SER30
3.307
GLY31
2.877
GLY32
4.168
VAL49
3.738
GLU50
2.677
SER51
3.090
HIS52
3.850
LYS53
3.696
GLY55
4.261
GLY56
3.214
THR57
2.656
CYS58
3.334
VAL61
3.715
GLY62
3.622
CYS63
3.254
LYS66
2.753
GLY128
3.387
HIS129
3.256
ALA130
3.004
ALA155
3.352
THR156
3.367
GLY157
3.358
GLY158
4.221
SER177
3.852
PHE181
4.239
TYR197
3.158
ILE198
3.909
GLU201
4.580
MET202
3.928
ARG291
3.398
ASN294
3.540
LEU298
3.604
VAL329
4.325
GLY330
3.432
ASP331
2.789
VAL332
4.555
LEU337
3.286
LEU338
3.131
THR339
3.004
PRO340
3.085
ALA342
4.004
PHE372
4.184
|
|||||
| PDB ID: 3GRS REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 1.54 Å | Mutation | No | [3] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.830
GLY27
3.253
GLY28
3.964
GLY29
3.408
SER30
3.352
GLY31
2.742
GLY32
4.061
VAL49
3.665
GLU50
2.654
SER51
3.133
HIS52
3.545
LYS53
3.730
GLY55
4.489
GLY56
3.155
THR57
2.854
CYS58
3.469
VAL61
3.629
GLY62
3.539
CYS63
3.425
LYS66
2.783
GLY128
3.374
HIS129
3.245
ALA130
2.896
ALA155
3.488
THR156
3.330
GLY157
3.345
GLY158
4.302
SER177
3.942
PHE181
4.331
TYR197
3.125
ILE198
4.004
GLU201
4.817
ARG291
3.509
ASN294
4.310
LEU298
3.763
VAL329
4.280
GLY330
3.528
ASP331
2.765
VAL332
4.554
LEU337
3.268
LEU338
3.118
THR339
3.098
PRO340
3.177
ALA342
3.932
PHE372
4.408
|
|||||
| PDB ID: 1DNC HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [4] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNCTEEL238 ENAGVEVLKF248 SQVKEVKKTL258 SGLEVSMVTA268 VPGRLPVMTM 278 IPDVDCLLWA288 IGRVPNTKDL298 SLNKLGIQTD308 DKGHIIVDEF318 QNTNVKGIYA 328 VGDVCGKALL338 TPVAIAAGRK348 LAHRLFEYKE358 DSKLDYNNIP368 TVVFSHPPIG 378 TVGLTEDEAI388 HKYGIENVKT398 YSTSFTPMYH408 AVTKRKTKCV418 MKMVCANKEE 428 KVVGIHMQGL438 GCDEMLQGFA448 VAVKMGATKA458 DFDNTVAIHP468 TSSEELVTLR 478
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.814
GLY27
3.243
GLY28
3.779
GLY29
3.475
SER30
3.351
GLY31
2.969
GLY32
4.321
VAL49
3.743
GLU50
2.700
SER51
3.173
HIS52
3.224
LYS53
3.793
GLY55
4.684
GLY56
3.504
THR57
2.855
CYS58
3.717
VAL61
3.703
GLY62
3.680
LYS66
2.801
GLY128
3.304
HIS129
3.191
ALA130
2.887
ALA155
3.496
THR156
3.281
GLY157
3.414
GLY158
4.221
SER177
3.939
PHE181
4.433
TYR197
3.110
ILE198
4.076
GLU201
4.662
ARG291
3.487
ASN294
4.574
LEU298
3.513
VAL329
4.411
GLY330
3.230
ASP331
2.690
VAL332
4.586
LEU337
3.243
LEU338
3.144
THR339
3.037
PRO340
3.192
ALA342
4.181
PHE372
4.279
|
|||||
| PDB ID: 1GSN HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [4] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNTEELE239 NAGVEVLKFS249 QVKEVKKTLS259 GLEVSMVTAV269 PGRLPVMTMI 279 PDVDLLWAIG290 RVPNTKDLSL300 NKLGIQTDDK310 GHIIVDEFQN320 TNVKGIYAVG 330 DVCGKALLTP340 VAIAAGRKLA350 HRLFEYKEDS360 KLDYNNIPTV370 VFSHPPIGTV 380 GLTEDEAIHK390 YGIENVKTYS400 TSFTPMYHAV410 TKRKTKCVMK420 MVANKEEKVV 431 GIHMQGLGCD441 EMLQGFAVAV451 KMGATKADFD461 NTVAIHPTSS471 EELVTLR |
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.802
GLY27
3.182
GLY28
3.769
GLY29
3.354
SER30
3.372
GLY31
2.927
GLY32
4.237
VAL49
3.775
GLU50
2.618
SER51
3.161
HIS52
3.410
LYS53
3.790
GLY55
4.605
GLY56
3.370
THR57
2.914
CYS58
3.561
VAL61
3.785
GLY62
3.784
LYS66
2.917
GLY128
3.291
HIS129
3.204
ALA130
3.005
ALA155
3.430
THR156
3.252
GLY157
3.340
GLY158
4.251
SER177
4.022
PHE181
4.367
TYR197
3.234
ILE198
4.105
GLU201
4.544
ARG291
3.553
ASN294
4.383
LEU298
3.765
VAL329
4.329
GLY330
3.240
ASP331
2.698
VAL332
4.548
LEU337
3.329
LEU338
3.229
THR339
2.941
PRO340
3.043
ALA342
4.074
PHE372
4.080
|
|||||
| PDB ID: 2GH5 Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5 | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [5] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.751
GLY27
3.228
GLY28
3.959
GLY29
3.434
SER30
3.238
GLY31
2.863
GLY32
4.342
VAL49
3.345
GLU50
2.720
SER51
3.284
HIS52
3.350
LYS53
3.872
GLY55
4.289
GLY56
3.285
THR57
2.720
CYS58
3.472
VAL61
3.771
GLY62
3.679
CYS63
3.245
LYS66
2.794
GLY128
3.382
HIS129
3.082
ALA130
3.010
ALA155
3.405
THR156
3.360
GLY157
3.334
GLY158
4.160
SER177
3.903
PHE181
4.152
TYR197
3.102
ILE198
3.806
GLU201
4.531
ARG291
3.327
ASN294
4.566
LEU298
4.701
VAL329
4.375
GLY330
3.305
ASP331
2.790
VAL332
4.560
LEU337
3.318
LEU338
3.262
THR339
2.987
PRO340
3.085
ALA342
3.987
PHE372
3.929
|
|||||
| PDB ID: 1GRB SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 1.85 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.815
GLY27
3.255
GLY28
3.997
GLY29
3.289
SER30
3.238
GLY31
2.883
GLY32
4.207
VAL49
3.729
GLU50
2.623
SER51
3.184
HIS52
3.402
LYS53
3.756
GLY55
4.332
GLY56
3.219
THR57
2.841
CYS58
3.472
VAL61
3.638
GLY62
3.471
CYS63
3.206
LYS66
2.755
GLY128
3.389
HIS129
3.360
ALA130
3.025
ALA155
3.438
THR156
3.252
GLY157
3.493
GLY158
4.249
SER177
3.951
PHE181
4.220
ILE198
3.962
GLU201
4.658
ARG291
3.657
ASN294
4.286
LEU298
3.827
VAL329
4.346
GLY330
3.419
ASP331
2.691
VAL332
4.494
LEU337
3.289
LEU338
3.214
THR339
3.145
PRO340
3.157
ALA342
4.046
PHE372
3.891
|
|||||
| PDB ID: 1GRA SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.925
GLY27
3.250
GLY28
3.943
GLY29
3.286
SER30
3.364
GLY31
2.776
GLY32
4.053
VAL49
3.788
GLU50
2.599
SER51
3.144
HIS52
3.462
LYS53
3.814
GLY55
4.344
GLY56
3.136
THR57
2.750
CYS58
3.418
VAL61
3.563
GLY62
3.496
CYS63
3.415
LYS66
2.754
GLY128
3.420
HIS129
3.147
ALA130
2.952
ALA155
3.430
THR156
3.292
GLY157
3.308
GLY158
4.154
SER177
3.948
PHE181
4.241
TYR197
3.142
ILE198
4.072
GLU201
4.865
ARG291
3.501
ASN294
4.206
LEU298
3.717
VAL329
4.158
GLY330
3.417
ASP331
2.804
VAL332
4.422
LEU337
3.280
LEU338
3.148
THR339
3.154
PRO340
3.146
ALA342
4.037
PHE372
4.431
|
|||||
| PDB ID: 1GRE SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.900
GLY27
3.188
GLY28
3.827
GLY29
3.435
SER30
3.348
GLY31
2.905
GLY32
4.240
VAL49
3.650
GLU50
2.601
SER51
3.150
HIS52
3.438
LYS53
3.696
GLY55
4.440
GLY56
3.224
THR57
2.914
CYS58
3.419
VAL61
3.576
GLY62
3.519
CYS63
3.288
LYS66
2.660
GLY128
3.362
HIS129
3.241
ALA130
2.931
ALA155
3.545
THR156
3.197
GLY157
3.325
GLY158
4.200
SER177
4.003
PHE181
4.278
TYR197
3.049
ILE198
4.144
GLU201
4.738
ARG291
3.469
ASN294
4.534
LEU298
3.715
VAL329
4.286
GLY330
3.406
ASP331
2.704
VAL332
4.559
LEU337
3.223
LEU338
3.117
THR339
3.125
PRO340
3.119
ALA342
4.119
PHE372
4.299
|
|||||
| PDB ID: 1GRF SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.782
GLY27
3.191
GLY28
3.900
GLY29
3.380
SER30
3.285
GLY31
2.840
GLY32
4.292
VAL49
3.707
GLU50
2.614
SER51
3.113
HIS52
3.440
LYS53
3.755
GLY55
4.248
GLY56
3.265
THR57
2.904
CYS58
3.455
VAL61
3.588
GLY62
3.517
CYS63
3.210
LYS66
2.728
GLY128
3.314
HIS129
3.340
ALA130
2.944
ALA155
3.414
THR156
3.267
GLY157
3.401
GLY158
4.287
SER177
4.054
PHE181
4.265
TYR197
3.106
ILE198
4.085
GLU201
4.697
ARG291
3.475
ASN294
4.403
LEU298
3.820
VAL329
4.327
GLY330
3.411
ASP331
2.560
VAL332
4.563
LEU337
3.196
LEU338
3.072
THR339
3.146
PRO340
3.172
ALA342
4.067
PHE372
4.265
|
|||||
| PDB ID: 1GRG SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 VNVGCVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNCTEEL238 ENAGVEVLKF248 SQVKEVKKTL258 SGLEVSMVTA268 VPGRLPVMTM 278 IPDVDCLLWA288 IGRVPNTKDL298 SLNKLGIQTD308 DKGHIIVDEF318 QNTNVKGIYA 328 VGDVCGKALL338 TPVAIAAGRK348 LAHRLFEYKE358 DSKLDYNNIP368 TVVFSHPPIG 378 TVGLTEDEAI388 HKYGIENVKT398 YSTSFTPMYH408 AVTKRKTKCV418 MKMVCANKEE 428 KVVGIHMQGL438 GCDEMLQGFA448 VAVKMGATKA458 DFDNTVAIHP468 TSSEELVTLR 478
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.866
GLY27
3.187
GLY28
3.929
GLY29
3.360
SER30
3.254
GLY31
2.765
GLY32
4.184
VAL49
3.709
GLU50
2.636
SER51
3.097
HIS52
3.506
LYS53
3.740
GLY55
4.144
GLY56
3.314
THR57
2.753
VAL61
3.611
GLY62
3.602
CYS63
3.286
LYS66
2.732
GLY128
3.318
HIS129
3.238
ALA130
2.922
ALA155
3.440
THR156
3.316
GLY157
3.390
GLY158
4.169
SER177
4.002
PHE181
4.277
TYR197
3.038
ILE198
4.047
GLU201
4.625
ARG291
3.458
ASN294
4.376
LEU298
3.808
VAL329
4.395
GLY330
3.552
ASP331
2.570
VAL332
4.631
LEU337
3.258
LEU338
3.167
THR339
3.095
PRO340
3.242
ALA342
4.062
PHE372
4.266
|
|||||
| PDB ID: 1BWC STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [7] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.868
GLY27
3.195
GLY28
4.002
GLY29
3.402
SER30
3.309
GLY31
2.821
GLY32
4.075
VAL49
3.697
GLU50
2.840
SER51
3.139
HIS52
3.384
LYS53
3.753
GLY55
4.513
GLY56
3.136
THR57
2.836
CYS58
3.457
VAL61
3.767
GLY62
3.703
CYS63
3.382
LYS66
2.922
GLY128
3.264
HIS129
3.172
ALA130
3.092
ALA155
3.256
THR156
3.331
GLY157
3.375
GLY158
4.123
SER177
4.100
PHE181
4.577
TYR197
3.168
ILE198
3.959
GLU201
4.750
ARG291
3.554
ASN294
3.519
LEU298
3.717
VAL329
4.446
GLY330
3.660
ASP331
2.878
VAL332
4.641
LEU337
3.379
LEU338
3.229
THR339
2.999
PRO340
3.160
ALA342
3.769
PHE372
4.158
|
|||||
| PDB ID: 3SQP Structure of human glutathione reductase complexed with pyocyanin, an agent with antimalarial activity | ||||||
| Method | X-ray diffraction | Resolution | 2.21 Å | Mutation | No | [8] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.822
GLY27
3.072
GLY28
3.979
GLY29
3.129
SER30
3.345
GLY31
2.785
GLY32
3.901
VAL49
3.705
GLU50
2.741
SER51
3.190
HIS52
3.523
LYS53
3.645
GLY55
4.109
GLY56
3.107
THR57
2.676
CYS58
3.371
VAL61
3.524
GLY62
3.522
CYS63
3.198
LYS66
2.672
GLY128
3.178
HIS129
3.072
ALA130
2.818
ALA155
3.275
THR156
3.196
GLY157
3.188
GLY158
4.571
SER177
3.575
PHE181
4.024
TYR197
3.168
ILE198
3.935
GLU201
4.669
ARG291
3.265
ASN294
3.761
LEU298
3.648
VAL329
4.096
GLY330
3.324
ASP331
2.796
VAL332
4.515
LEU337
3.305
LEU338
3.254
THR339
2.814
PRO340
2.661
ALA342
3.602
PHE372
4.056
|
|||||
| PDB ID: 1GRT HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [9] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLESA36 WRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.742
GLY27
3.137
GLY28
3.703
GLY29
3.369
SER30
3.545
GLY31
2.891
GLY32
4.100
VAL49
3.890
GLU50
2.908
SER51
3.084
HIS52
3.059
LYS53
3.471
GLY55
3.922
GLY56
3.049
THR57
2.695
CYS58
3.340
VAL61
3.728
GLY62
3.506
CYS63
3.391
LYS66
2.603
GLY128
3.523
HIS129
3.274
ALA130
3.020
ALA155
3.285
THR156
3.001
GLY157
3.495
GLY158
4.413
SER177
3.906
PHE181
4.253
TYR197
3.319
ILE198
3.908
GLU201
4.846
ARG291
3.744
ASN294
3.364
LEU298
3.363
VAL329
3.975
GLY330
3.582
ASP331
2.629
VAL332
4.236
LEU337
3.489
LEU338
3.154
THR339
3.254
PRO340
3.089
ALA342
3.931
PHE372
4.375
|
|||||
| PDB ID: 4GR1 THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [10] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.850
GLY27
3.317
GLY28
3.862
GLY29
3.305
SER30
3.392
GLY31
2.691
GLY32
4.246
VAL49
3.764
GLU50
2.536
SER51
3.230
HIS52
3.540
LYS53
3.853
GLY55
4.466
GLY56
3.093
THR57
2.939
CYS58
3.497
VAL61
3.635
GLY62
3.497
CYS63
3.482
LYS66
2.779
GLY128
3.454
HIS129
3.262
ALA130
2.823
ALA155
3.455
THR156
3.285
GLY157
3.487
GLY158
4.271
SER177
3.936
PHE181
4.348
TYR197
3.152
ILE198
3.956
GLU201
4.691
ARG291
3.622
ASN294
4.294
LEU298
3.576
VAL329
4.097
GLY330
3.567
ASP331
2.740
VAL332
4.403
LEU337
3.320
LEU338
3.122
THR339
3.208
PRO340
3.267
ALA342
3.793
PHE372
4.549
|
|||||
| PDB ID: 1GRH INHIBITION OF HUMAN GLUTATHIONE REDUCTASE BY THE NITROSOUREA DRUGS 1,3-BIS(2-CHLOROETHYL)-1-NITROSOUREA AND 1-(2-CHLOROETHYL)-3-(2-HYDROXYETHYL)-1-NITROSOUREA | ||||||
| Method | X-ray diffraction | Resolution | 3.00 Å | Mutation | No | [11] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.866
GLY27
3.187
GLY28
3.929
GLY29
3.360
SER30
3.254
GLY31
2.765
GLY32
4.184
VAL49
3.709
GLU50
2.636
SER51
3.097
HIS52
3.506
LYS53
3.740
GLY55
4.144
GLY56
3.314
THR57
2.753
CYS58
3.310
VAL61
3.611
GLY62
3.602
CYS63
3.286
LYS66
2.732
GLY128
3.318
HIS129
3.238
ALA130
2.922
ALA155
3.440
THR156
3.316
GLY157
3.390
GLY158
4.169
SER177
4.002
PHE181
4.277
TYR197
3.038
ILE198
4.047
GLU201
4.625
ARG291
3.458
ASN294
4.376
LEU298
3.808
VAL329
4.395
GLY330
3.552
ASP331
2.570
VAL332
4.631
LEU337
3.258
LEU338
3.167
THR339
3.095
PRO340
3.242
ALA342
4.062
PHE372
4.266
|
|||||
| PDB ID: 3DJG Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [2] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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 .X:26 or .X:27 or .X:28 or .X:29 or .X:30 or .X:31 or .X:32 or .X:49 or .X:50 or .X:51 or .X:52 or .X:53 or .X:55 or .X:56 or .X:57 or .X:58 or .X:61 or .X:62 or .X:63 or .X:66 or .X:128 or .X:129 or .X:130 or .X:155 or .X:156 or .X:157 or .X:158 or .X:177 or .X:181 or .X:198 or .X:201 or .X:291 or .X:294 or .X:298 or .X:329 or .X:330 or .X:331 or .X:332 or .X:337 or .X:338 or .X:339 or .X:340 or .X:342 or .X:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.862
GLY27
3.321
GLY28
3.973
GLY29
3.250
SER30
3.232
GLY31
2.845
GLY32
4.237
VAL49
3.655
GLU50
2.641
SER51
3.271
HIS52
3.526
LYS53
3.773
GLY55
4.194
GLY56
3.254
THR57
2.691
CYS58
3.474
VAL61
3.762
GLY62
3.614
CYS63
3.159
LYS66
2.726
GLY128
3.413
HIS129
3.363
ALA130
3.067
ALA155
3.407
THR156
3.351
GLY157
3.439
GLY158
4.302
SER177
3.928
PHE181
4.414
ILE198
3.911
GLU201
4.754
ARG291
3.406
ASN294
3.707
LEU298
3.553
VAL329
4.414
GLY330
3.380
ASP331
2.704
VAL332
4.581
LEU337
3.296
LEU338
3.156
THR339
3.094
PRO340
3.190
ALA342
4.028
PHE372
3.703
|
|||||
| PDB ID: 1K4Q Human Glutathione Reductase Inactivated by Peroxynitrite | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | Yes | [12] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:297 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.790
GLY27
3.324
GLY28
3.917
GLY29
3.370
SER30
3.412
GLY31
2.902
GLY32
4.163
VAL49
3.572
GLU50
2.592
SER51
2.994
HIS52
3.535
LYS53
3.870
GLY55
4.409
GLY56
3.274
THR57
2.838
CYS58
3.320
VAL61
3.776
GLY62
3.705
CYS63
3.445
LYS66
2.762
GLY128
3.332
HIS129
3.120
ALA130
2.968
ALA155
3.416
THR156
3.350
GLY157
3.455
GLY158
4.388
SER177
3.969
PHE181
4.366
TYR197
3.217
ILE198
4.140
GLU201
4.750
ARG291
3.536
ASN294
4.497
ASP297
4.986
LEU298
3.790
VAL329
4.286
GLY330
3.344
ASP331
2.888
VAL332
4.538
LEU337
3.461
LEU338
3.247
THR339
3.128
PRO340
3.090
ALA342
3.791
PHE372
4.615
|
|||||
| PDB ID: 1XAN HUMAN GLUTATHIONE REDUCTASE IN COMPLEX WITH A XANTHENE INHIBITOR | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [13] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.911
GLY27
3.138
GLY28
3.887
GLY29
3.341
SER30
3.368
GLY31
2.851
GLY32
4.105
VAL49
3.681
GLU50
2.618
SER51
3.203
HIS52
3.428
LYS53
3.799
GLY55
4.440
GLY56
3.331
THR57
2.840
CYS58
3.534
VAL61
3.772
GLY62
3.626
CYS63
3.509
LYS66
2.798
GLY128
3.314
HIS129
3.272
ALA130
2.934
ALA155
3.334
THR156
3.394
GLY157
3.441
GLY158
4.243
SER177
3.981
PHE181
4.364
TYR197
3.165
ILE198
3.994
GLU201
4.691
ARG291
3.607
ASN294
4.367
LEU298
3.471
VAL329
4.258
GLY330
3.294
ASP331
2.788
VAL332
4.582
LEU337
3.299
LEU338
3.124
THR339
3.075
PRO340
3.145
ALA342
4.023
PHE372
4.274
|
|||||
| PDB ID: 5GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [9] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:202 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.748
GLY27
3.240
GLY28
3.883
GLY29
3.149
SER30
3.570
GLY31
2.791
GLY32
4.027
VAL49
3.353
GLU50
2.739
SER51
3.054
HIS52
3.113
LYS53
3.527
GLY55
4.294
GLY56
3.370
THR57
2.784
CYS58
3.386
VAL61
3.721
GLY62
3.690
CYS63
3.638
LYS66
2.648
GLY128
3.496
HIS129
3.293
ALA130
3.040
ALA155
3.484
THR156
3.313
GLY157
3.617
GLY158
4.507
SER177
3.913
PHE181
4.331
TYR197
3.267
ILE198
4.048
GLU201
4.784
MET202
4.260
ARG291
3.506
ASN294
4.104
LEU298
3.652
VAL329
3.746
GLY330
3.240
ASP331
2.565
VAL332
4.325
LEU337
3.475
LEU338
3.467
THR339
3.156
PRO340
3.555
ALA342
3.693
PHE372
4.320
|
|||||
| PDB ID: 3GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | Yes | [9] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.699
GLY27
3.080
GLY28
3.560
GLY29
3.301
SER30
3.378
GLY31
2.865
GLY32
3.930
VAL49
3.238
GLU50
2.746
SER51
3.051
HIS52
3.516
LYS53
3.433
GLY55
4.399
GLY56
3.412
THR57
3.050
CYS58
3.446
VAL61
3.672
GLY62
3.629
CYS63
3.346
LYS66
3.086
GLY128
3.209
HIS129
3.326
ALA130
3.060
ALA155
3.511
THR156
3.369
GLY157
3.572
GLY158
4.327
SER177
4.228
PHE181
4.433
TYR197
3.200
ILE198
4.034
GLU201
4.842
ARG291
3.318
ASN294
3.816
LEU298
4.078
VAL329
3.767
GLY330
3.347
ASP331
2.546
VAL332
4.331
LEU337
3.471
LEU338
3.207
THR339
3.313
PRO340
4.107
ALA342
3.673
PHE372
4.619
|
|||||
| PDB ID: 2GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | Yes | [9] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:202 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.433
GLY27
3.374
GLY28
3.955
GLY29
3.294
SER30
3.324
GLY31
2.880
GLY32
3.957
VAL49
3.870
GLU50
2.625
SER51
3.167
HIS52
3.095
LYS53
3.678
GLY55
4.530
GLY56
3.321
THR57
3.021
CYS58
3.510
VAL61
3.545
GLY62
3.460
CYS63
3.479
LYS66
2.730
GLY128
3.371
HIS129
3.009
ALA130
2.970
ALA155
3.349
THR156
3.289
GLY157
3.522
GLY158
4.363
SER177
4.043
PHE181
4.392
TYR197
3.406
ILE198
4.140
GLU201
4.784
MET202
4.283
ARG291
3.630
ASN294
3.936
LEU298
3.745
VAL329
3.772
GLY330
3.295
ASP331
2.607
VAL332
4.263
LEU337
3.539
LEU338
3.516
THR339
3.091
PRO340
3.353
ALA342
3.686
PHE372
4.438
|
|||||
| PDB ID: 4GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | Yes | [9] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
|
|||||
|
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:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:56 or .A:57 or .A:58 or .A:61 or .A:62 or .A:63 or .A:66 or .A:128 or .A:129 or .A:130 or .A:155 or .A:156 or .A:157 or .A:158 or .A:177 or .A:181 or .A:197 or .A:198 or .A:201 or .A:202 or .A:291 or .A:294 or .A:298 or .A:329 or .A:330 or .A:331 or .A:332 or .A:337 or .A:338 or .A:339 or .A:340 or .A:342 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE26
3.227
GLY27
3.346
GLY28
3.529
GLY29
3.658
SER30
3.437
GLY31
2.737
VAL49
3.069
GLU50
2.642
SER51
2.910
HIS52
2.669
LYS53
3.012
GLY56
3.258
THR57
2.892
CYS58
3.722
VAL61
3.604
GLY62
3.667
CYS63
3.115
LYS66
2.999
GLY128
3.635
HIS129
3.077
ALA130
3.209
ALA155
3.752
THR156
3.071
GLY157
2.972
GLY158
3.507
SER177
4.151
PHE181
4.293
TYR197
3.509
ILE198
3.871
GLU201
4.403
MET202
4.438
ARG291
4.101
ASN294
4.230
LEU298
3.779
VAL329
4.042
GLY330
3.524
ASP331
2.509
VAL332
4.450
LEU337
3.645
LEU338
3.259
THR339
2.768
PRO340
3.086
ALA342
3.626
PHE372
4.635
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases. Angew Chem Int Ed Engl. 2006 Mar 13;45(12):1881-6. | ||||
| REF 2 | Catalytic cycle of human glutathione reductase near 1 A resolution. J Mol Biol. 2008 Oct 3;382(2):371-84. | ||||
| REF 3 | Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. | ||||
| REF 4 | Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. | ||||
| REF 5 | A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme. J Am Chem Soc. 2006 Aug 23;128(33):10784-94. | ||||
| REF 6 | Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. J Mol Biol. 1989 Nov 5;210(1):163-80. | ||||
| REF 7 | Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies. J Med Chem. 1999 Feb 11;42(3):364-72. | ||||
| REF 8 | The bacterial redox signaller pyocyanin as an antiplasmodial agent: comparisons with its thioanalog methylene blue. Redox Rep. 2011;16(4):154-65. | ||||
| REF 9 | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. | ||||
| REF 10 | The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J Biol Chem. 1990 Jun 25;265(18):10443-5. | ||||
| REF 11 | Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis. Eur J Biochem. 1988 Jan 15;171(1-2):193-8. | ||||
| REF 12 | Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite. J Biol Chem. 2002 Jan 25;277(4):2779-84. | ||||
| REF 13 | Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. | ||||
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