Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T93062 | Target Info | |||
| Target Name | Multidrug resistance protein 3 (ABCB4) | ||||
| Synonyms | PGY3; MDR3; ATP-binding cassette sub-family B member 4; ABCB4 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | ABCB4 | ||||
| Biochemical Class | Acid anhydrides hydrolase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Adenosine triphosphate | Ligand Info | |||||
| Structure Description | Nucleotide bound ABCB4 | PDB:6S7P | ||||
| Method | Electron microscopy | Resolution | 3.20 Å | Mutation | Yes | [1] |
| PDB Sequence |
VLTLFRYSDW
51 QDKLFMSLGT61 IMAIAHGSGL71 PLMMIVFGEM81 TDKPGKILEE111 EMTRYAYYYS 121 GLGAGVLVAA131 YIQVSFWTLA141 AGRQIRKIRQ151 KFFHAILRQE161 IGWFDINDTT 171 ELNTRLTDDI181 SKISEGIGDK191 VGMFFQAVAT201 FFAGFIVGFI211 RGWKLTLVIM 221 AISPILGLSA231 AVWAKILSAF241 SDKELAAYAK251 AGAVAEEALG261 AIRTVIAFGG 271 QNKELERYQK281 HLENAKEIGI291 KKAISANISM301 GIAFLLIYAS311 YALAFWYGST 321 LVISKEYTIG331 NAMTVFFSIL341 IGAFSVGQAA351 PCIDAFANAR361 GAAYVIFDII 371 DNNPKIDSFS381 ERGHKPDSIK391 GNLEFNDVHF401 SYPSRANVKI411 LKGLNLKVQS 421 GQTVALVGSS431 GCGKSTTVQL441 IQRLYDPDEG451 TINIDGQDIR461 NFNVNYLREI 471 IGVVSQEPVL481 FSTTIAENIC491 YGRGNVTMDE501 IKKAVKEANA511 YEFIMKLPQK 521 FDTLVGERGA531 QLSGGQKQRI541 AIARALVRNP551 KILLLDQATS561 ALDTESEAEV 571 QAALDKAREG581 RTTIVIAHRL591 STVRNADVIA601 GFEDGVIVEQ611 GSHSELMKKE 621 GVYFKLVNVP693 PVSFLKVLKL703 NKTEWPYFVV713 GTVCAIANGG723 LQPAFSVIFS 733 EIIAIFGPGD743 DAVKQQKCNI753 FSLIFLFLGI763 ISFFTFFLQG773 FTFGKAGEIL 783 TRRLRSMAFK793 AMLRQDMSWF803 DDHKNSTGAL813 STRLATDAAQ823 VQGATGTRLA 833 LIAQNIANLG843 TGIIISFIYG853 WQLTLLLLAV863 VPIIAVSGIV873 EMKLLAGNAK 883 RDKKELEAAG893 KIATEAIENI903 RTVVSLTQER913 KFESMYVEKL923 YGPYRNSVQK 933 AHIYGITFSI943 SQAFMYFSYA953 GCFRFGAYLI963 VNGHMRFRDV973 ILVFSAIVFG 983 AVALGHASSF993 APDYAKAKLS1003 AAHLFMLFER1013 QPLIDSYSEE1023 GLKPDKFEGN 1033 ITFNEVVFNY1043 PTRANVPVLQ1053 GLSLEVKKGQ1063 TLALVGSSGC1073 GKSTVVQLLE 1083 RFYDPLAGTV1093 LLDGQEAKKL1103 NVQWLRAQLG1113 IVSQEPILFD1123 CSIAENIAYG 1133 DNSRVVSQDE1143 IVSAAKAANI1153 HPFIETLPHK1163 YETRVGDKGT1173 QLSGGQKQRI 1183 AIARALIRQP1193 QILLLDQATS1203 ALDTESEKVV1213 QEALDKAREG1223 RTCIVIAHRL 1233 STIQNADLIV1243 VFQNGRVK
|
|||||
|
|
ASP166
3.995
ARG264
4.078
TYR403
3.555
SER405
3.167
ARG406
2.770
ILE411
3.371
SER430
4.113
SER431
4.094
GLY432
3.100
CYS433
3.379
GLY434
3.225
LYS435
2.881
SER436
2.492
THR437
3.141
TYR446
4.209
GLN477
2.513
ALA531
3.546
GLN532
3.711
LEU533
4.154
SER534
3.279
GLY535
3.400
GLY536
3.069
GLN537
3.495
ASP557
3.347
ALA562
4.250
ILE587
4.641
ASP804
3.831
ARG904
3.847
TYR1043
3.571
THR1045
3.203
ARG1046
2.991
VAL1051
4.219
SER1070
4.226
SER1071
2.820
GLY1072
3.280
CYS1073
3.427
GLY1074
3.496
LYS1075
2.347
SER1076
3.068
THR1077
3.230
TYR1086
4.364
GLN1117
2.583
PHE1156
3.630
THR1173
3.334
GLN1174
3.684
LEU1175
4.191
SER1176
3.246
GLY1177
3.077
GLY1178
4.369
GLN1179
3.308
GLN1200
4.845
|
|||||
| Ligand Name: Posaconazole | Ligand Info | |||||
| Structure Description | Nanodisc reconstituted human ABCB4 in complex with 4B1-Fab (posaconazole-bound, inward-open conformation) | PDB:7NIW | ||||
| Method | Electron microscopy | Resolution | 3.80 Å | Mutation | Yes | [2] |
| PDB Sequence |
TLFRYSDWQD
53 KLFMSLGTIM63 AIAHGSGLPL73 MMIVFGEMTD83 KFVDTAGNFS93 FPVPGKILEE 111 EMTRYAYYYS121 GLGAGVLVAA131 YIQVSFWTLA141 AGRQIRKIRQ151 KFFHAILRQE 161 IGWFDINDTT171 ELNTRLTDDI181 SKISEGIGDK191 VGMFFQAVAT201 FFAGFIVGFI 211 RGWKLTLVIM221 AISPILGLSA231 AVWAKILSAF241 SDKELAAYAK251 AGAVAEEALG 261 AIRTVIAFGG271 QNKELERYQK281 HLENAKEIGI291 KKAISANISM301 GIAFLLIYAS 311 YALAFWYGST321 LVISKEYTIG331 NAMTVFFSIL341 IGAFSVGQAA351 PCIDAFANAR 361 GAAYVIFDII371 DNNPKIDSFS381 ERGHKPDSIK391 GNLEFNDVHF401 SYPSRANVKI 411 LKGLNLKVQS421 GQTVALVGSS431 GCGKSTTVQL441 IQRLYDPDEG451 TINIDGQDIR 461 NFNVNYLREI471 IGVVSQEPVL481 FSTTIAENIC491 YGRGNVTMDE501 IKKAVKEANA 511 YEFIMKLPQK521 FDTLVGERGA531 QLSGGQKQRI541 AIARALVRNP551 KILLLDQATS 561 ALDTESEAEV571 QAALDKAREG581 RTTIVIAHRL591 STVRNADVIA601 GFEDGVIVEQ 611 GSHSELMKKE621 GVYFKLVNAN691 VPPVSFLKVL701 KLNKTEWPYF711 VVGTVCAIAN 721 GGLQPAFSVI731 FSEIIAIFGP741 GDDAVKQQKC751 NIFSLIFLFL761 GIISFFTFFL 771 QGFTFGKAGE781 ILTRRLRSMA791 FKAMLRQDMS801 WFDDHKNSTG811 ALSTRLATDA 821 AQVQGATGTR831 LALIAQNIAN841 LGTGIIISFI851 YGWQLTLLLL861 AVVPIIAVSG 871 IVEMKLLAGN881 AKRDKKELEA891 AGKIATEAIE901 NIRTVVSLTQ911 ERKFESMYVE 921 KLYGPYRNSV931 QKAHIYGITF941 SISQAFMYFS951 YAGCFRFGAY961 LIVNGHMRFR 971 DVILVFSAIV981 FGAVALGHAS991 SFAPDYAKAK1001 LSAAHLFMLF1011 ERQPLIDSYS 1021 EEGLKPDKFE1031 GNITFNEVVF1041 NYPTRANVPV1051 LQGLSLEVKK1061 GQTLALVGSS 1071 GCGKSTVVQL1081 LERFYDPLAG1091 TVLLDGQEAK1101 KLNVQWLRAQ1111 LGIVSQEPIL 1121 FDCSIAENIA1131 YGDNSRVVSQ1141 DEIVSAAKAA1151 NIHPFIETLP1161 HKYETRVGDK 1171 GTQLSGGQKQ1181 RIAIARALIR1191 QPQILLLDQA1201 TSALDTESEK1211 VVQEALDKAR 1221 EGRTCIVIAH1231 RLSTIQNADL1241 IVVFQNGRVK1251
|
|||||
|
|
LEU71
4.155
MET75
2.911
ASN298
4.335
MET301
3.402
PHE305
4.728
PHE338
4.418
LEU341
3.349
ILE342
3.335
PHE345
3.109
SER346
4.867
GLN349
4.872
ASN721
4.424
GLN725
3.772
PHE769
3.250
|
|||||
| Ligand Name: Cholesterol | Ligand Info | |||||
| Structure Description | Nucleotide bound ABCB4 | PDB:6S7P | ||||
| Method | Electron microscopy | Resolution | 3.20 Å | Mutation | Yes | [1] |
| PDB Sequence |
VLTLFRYSDW
51 QDKLFMSLGT61 IMAIAHGSGL71 PLMMIVFGEM81 TDKPGKILEE111 EMTRYAYYYS 121 GLGAGVLVAA131 YIQVSFWTLA141 AGRQIRKIRQ151 KFFHAILRQE161 IGWFDINDTT 171 ELNTRLTDDI181 SKISEGIGDK191 VGMFFQAVAT201 FFAGFIVGFI211 RGWKLTLVIM 221 AISPILGLSA231 AVWAKILSAF241 SDKELAAYAK251 AGAVAEEALG261 AIRTVIAFGG 271 QNKELERYQK281 HLENAKEIGI291 KKAISANISM301 GIAFLLIYAS311 YALAFWYGST 321 LVISKEYTIG331 NAMTVFFSIL341 IGAFSVGQAA351 PCIDAFANAR361 GAAYVIFDII 371 DNNPKIDSFS381 ERGHKPDSIK391 GNLEFNDVHF401 SYPSRANVKI411 LKGLNLKVQS 421 GQTVALVGSS431 GCGKSTTVQL441 IQRLYDPDEG451 TINIDGQDIR461 NFNVNYLREI 471 IGVVSQEPVL481 FSTTIAENIC491 YGRGNVTMDE501 IKKAVKEANA511 YEFIMKLPQK 521 FDTLVGERGA531 QLSGGQKQRI541 AIARALVRNP551 KILLLDQATS561 ALDTESEAEV 571 QAALDKAREG581 RTTIVIAHRL591 STVRNADVIA601 GFEDGVIVEQ611 GSHSELMKKE 621 GVYFKLVNVP693 PVSFLKVLKL703 NKTEWPYFVV713 GTVCAIANGG723 LQPAFSVIFS 733 EIIAIFGPGD743 DAVKQQKCNI753 FSLIFLFLGI763 ISFFTFFLQG773 FTFGKAGEIL 783 TRRLRSMAFK793 AMLRQDMSWF803 DDHKNSTGAL813 STRLATDAAQ823 VQGATGTRLA 833 LIAQNIANLG843 TGIIISFIYG853 WQLTLLLLAV863 VPIIAVSGIV873 EMKLLAGNAK 883 RDKKELEAAG893 KIATEAIENI903 RTVVSLTQER913 KFESMYVEKL923 YGPYRNSVQK 933 AHIYGITFSI943 SQAFMYFSYA953 GCFRFGAYLI963 VNGHMRFRDV973 ILVFSAIVFG 983 AVALGHASSF993 APDYAKAKLS1003 AAHLFMLFER1013 QPLIDSYSEE1023 GLKPDKFEGN 1033 ITFNEVVFNY1043 PTRANVPVLQ1053 GLSLEVKKGQ1063 TLALVGSSGC1073 GKSTVVQLLE 1083 RFYDPLAGTV1093 LLDGQEAKKL1103 NVQWLRAQLG1113 IVSQEPILFD1123 CSIAENIAYG 1133 DNSRVVSQDE1143 IVSAAKAANI1153 HPFIETLPHK1163 YETRVGDKGT1173 QLSGGQKQRI 1183 AIARALIRQP1193 QILLLDQATS1203 ALDTESEKVV1213 QEALDKAREG1223 RTCIVIAHRL 1233 STIQNADLIV1243 VFQNGRVK
|
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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 .CLR or .CLR2 or .CLR3 or :3CLR;style chemicals stick;color identity;select .A:52 or .A:55 or .A:56 or .A:59 or .A:63 or .A:66 or .A:67 or .A:69 or .A:70 or .A:73 or .A:74 or .A:76 or .A:77 or .A:114 or .A:117 or .A:118 or .A:119 or .A:121 or .A:123 or .A:126 or .A:127 or .A:128 or .A:129 or .A:130 or .A:132 or .A:133 or .A:137 or .A:140 or .A:223 or .A:307 or .A:310 or .A:311 or .A:313 or .A:314 or .A:317 or .A:719 or .A:720 or .A:723 or .A:724 or .A:727 or .A:730 or .A:731 or .A:734 or .A:752 or .A:754 or .A:755 or .A:756 or .A:757 or .A:759 or .A:842 or .A:846 or .A:859 or .A:863 or .A:864 or .A:867 or .A:868 or .A:871 or .A:872 or .A:875 or .A:927 or .A:928 or .A:931 or .A:935 or .A:947 or .A:948 or .A:950 or .A:951 or .A:953 or .A:954 or .A:957 or .A:958 or .A:961 or .A:987 or .A:997; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
GLN52
3.576
LEU55
3.731
PHE56
3.732
LEU59
3.639
MET63
4.065
ALA66
3.342
HIS67
4.056
SER69
4.276
GLY70
4.446
LEU73
3.377
MET74
4.133
ILE76
3.645
VAL77
3.728
THR114
3.876
ALA117
4.083
TYR118
4.250
TYR119
4.192
SER121
3.517
LEU123
4.187
GLY126
3.716
VAL127
4.254
LEU128
4.453
VAL129
4.315
ALA130
3.604
TYR132
4.353
ILE133
4.280
PHE137
3.608
LEU140
3.956
ILE223
4.418
LEU307
3.765
ALA310
3.913
SER311
4.562
ALA313
4.129
LEU314
3.762
TRP317
4.440
ILE719
4.576
ALA720
3.657
GLY723
4.096
LEU724
3.728
ALA727
3.967
VAL730
4.140
ILE731
4.159
GLU734
4.237
ASN752
4.216
PHE754
3.946
SER755
3.126
LEU756
3.723
ILE757
3.724
LEU759
4.104
LEU842
4.027
ILE846
4.660
LEU859
4.420
VAL863
3.689
VAL864
4.200
ILE867
3.806
ALA868
4.174
GLY871
4.304
ILE872
3.709
MET875
3.981
TYR927
4.509
ARG928
4.903
VAL931
4.770
HIS935
3.717
PHE947
3.886
MET948
4.355
PHE950
3.582
SER951
3.995
ALA953
3.978
GLY954
3.907
ARG957
3.434
PHE958
3.786
TYR961
3.606
LEU987
3.758
TYR997
4.759
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 1,2-Dilinoleoyl-SN-glycero-3-phosphocholine | Ligand Info | |||||
| Structure Description | Nanodisc reconstituted human ABCB4 in complex with 4B1-Fab and QA2-Fab (phosphatidylcholine-bound, occluded conformation) | PDB:7NIV | ||||
| Method | Electron microscopy | Resolution | 3.60 Å | Mutation | No | [2] |
| PDB Sequence |
MIGVLTLFRY
48 SDWQDKLFMS58 LGTIMAIAHG68 SGLPLMMIVF78 GEMTDKFVDT88 AGNFGKILEE 111 EMTRYAYYYS121 GLGAGVLVAA131 YIQVSFWTLA141 AGRQIRKIRQ151 KFFHAILRQE 161 IGWFDINDTT171 ELNTRLTDDI181 SKISEGIGDK191 VGMFFQAVAT201 FFAGFIVGFI 211 RGWKLTLVIM221 AISPILGLSA231 AVWAKILSAF241 SDKELAAYAK251 AGAVAEEALG 261 AIRTVIAFGG271 QNKELERYQK281 HLENAKEIGI291 KKAISANISM301 GIAFLLIYAS 311 YALAFWYGST321 LVISKEYTIG331 NAMTVFFSIL341 IGAFSVGQAA351 PCIDAFANAR 361 GAAYVIFDII371 DNNPKIDSFS381 ERGHKPDSIK391 GNLEFNDVHF401 SYPSRANVKI 411 LKGLNLKVQS421 GQTVALVGSS431 GCGKSTTVQL441 IQRLYDPDEG451 TINIDGQDIR 461 NFNVNYLREI471 IGVVSQEPVL481 FSTTIAENIC491 YGRGNVTMDE501 IKKAVKEANA 511 YEFIMKLPQK521 FDTLVGERGA531 QLSGGQKQRI541 AIARALVRNP551 KILLLDEATS 561 ALDTESEAEV571 QAALDKAREG581 RTTIVIAHRL591 STVRNADVIA601 GFEDGVIVEQ 611 GSHSELMKKE621 GVYFKLVNVP693 PVSFLKVLKL703 NKTEWPYFVV713 GTVCAIANGG 723 LQPAFSVIFS733 EIIAIFGPGD743 DAVKQQKCNI753 FSLIFLFLGI763 ISFFTFFLQG 773 FTFGKAGEIL783 TRRLRSMAFK793 AMLRQDMSWF803 DDHKNSTGAL813 STRLATDAAQ 823 VQGATGTRLA833 LIAQNIANLG843 TGIIISFIYG853 WQLTLLLLAV863 VPIIAVSGIV 873 EMKLLAGNAK883 RDKKELEAAG893 KIATEAIENI903 RTVVSLTQER913 KFESMYVEKL 923 YGPYRNSVQK933 AHIYGITFSI943 SQAFMYFSYA953 GCFRFGAYLI963 VNGHMRFRDV 973 ILVFSAIVFG983 AVALGHASSF993 APDYAKAKLS1003 AAHLFMLFER1013 QPLIDSYSEE 1023 GLKPDKFEGN1033 ITFNEVVFNY1043 PTRANVPVLQ1053 GLSLEVKKGQ1063 TLALVGSSGC 1073 GKSTVVQLLE1083 RFYDPLAGTV1093 LLDGQEAKKL1103 NVQWLRAQLG1113 IVSQEPILFD 1123 CSIAENIAYG1133 DNSRVVSQDE1143 IVSAAKAANI1153 HPFIETLPHK1163 YETRVGDKGT 1173 QLSGGQKQRI1183 AIARALIRQP1193 QILLLDEATS1203 ALDTESEKVV1213 QEALDKAREG 1223 RTCIVIAHRL1233 STIQNADLIV1243 VFQNGRVK
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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 .DLP or .DLP2 or .DLP3 or :3DLP;style chemicals stick;color identity;select .A:75 or .A:78 or .A:230 or .A:231 or .A:234 or .A:305 or .A:308 or .A:312 or .A:315 or .A:316 or .A:319 or .A:320 or .A:323 or .A:333 or .A:334 or .A:337 or .A:338 or .A:341 or .A:342 or .A:345 or .A:349 or .A:725 or .A:728 or .A:732 or .A:735 or .A:736 or .A:739 or .A:758 or .A:952 or .A:974 or .A:977 or .A:978 or .A:982 or .A:985 or .A:986 or .A:989; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET75
4.298
PHE78
3.455
SER230
4.925
ALA231
3.577
TRP234
3.399
PHE305
3.704
ILE308
3.587
TYR312
3.688
ALA315
3.896
PHE316
3.793
GLY319
3.133
SER320
4.589
VAL323
4.538
ALA333
4.125
MET334
3.213
PHE337
3.311
PHE338
3.755
LEU341
4.287
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure of the human lipid exporter ABCB4 in a lipid environment. Nat Struct Mol Biol. 2020 Jan;27(1):62-70. | ||||
| REF 2 | Structures of ABCB4 provide insight into phosphatidylcholine translocation. Proc Natl Acad Sci U S A. 2021 Aug 17;118(33):e2106702118. | ||||
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