Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T56556 | Target Info | |||
| Target Name | ATP-binding cassette transporter G2 (ABCG2) | ||||
| Synonyms | Urate exporter; Placenta-specific ATP-binding cassette transporter; Mitoxantrone resistance-associated protein; MXR; CDw338; CD338; Breast cancer resistance protein; BCRP1; BCRP; ABCP | ||||
| Target Type | Successful Target | ||||
| Gene Name | ABCG2 | ||||
| Biochemical Class | ABC transporter | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Cholesterol | Ligand Info | |||
| Canonical SMILES | CC(C)CCCC(C)C1CCC2C1(CCC3C2CC=C4C3(CCC(C4)O)C)C | ||||
| InChI | 1S/C27H46O/c1-18(2)7-6-8-19(3)23-11-12-24-22-10-9-20-17-21(28)13-15-26(20,4)25(22)14-16-27(23,24)5/h9,18-19,21-25,28H,6-8,10-17H2,1-5H3/t19-,21+,22+,23-,24+,25+,26+,27-/m1/s1 | ||||
| InChIKey | HVYWMOMLDIMFJA-DPAQBDIFSA-N | ||||
| PubChem Compound ID | 5997 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 7NEQ Structure of tariquidar-bound ABCG2 | ||||||
| Method | Electron microscopy | Resolution | 3.12 Å | Mutation | No | [1] |
| PDB Sequence |
AVLSFHNICY
44 RVKEILSNIN68 GIMKPGLNAI78 LGPTGGGKSS88 LLDVLAARKD98 PSGLSGDVLI 108 NGAPRPANFK118 CNSGYVVQDD128 VVMGTLTVRE138 NLQFSAALRL148 ATTMTNHEKN 158 ERINRVIQEL168 GLDKVADSKV178 GTQFIRGVSG188 GERKRTSIGM198 ELITDPSILF 208 LDEPTTGLDS218 STANAVLLLL228 KRMSKQGRTI238 IFSIHQPRYS248 IFKLFDSLTL 258 LASGRLMFHG268 PAQEALGYFE278 SAGYHCEAYN288 NPADFFLDII298 NGDLIEKLAE 334 IYVNSSFYKE344 TKAELHQLSG354 YTTSFCHQLR378 WVSKRSFKNL388 LGNPQASIAQ 398 IIVTVVLGLV408 IGAIYFGLKN418 DSTGIQNRAG428 VLFFLTTNQC438 FSSVSAVELF 448 VVEKKLFIHE458 YISGYYRVSS468 YFLGKLLSDL478 LPMRMLPSII488 FTCIVYFMLG 498 LKPKADAFFV508 MMFTLMMVAY518 SASSMALAIA528 AGQSVVSVAT538 LLMTICFVFM 548 MIFSGLLVNL558 TTIASWLSWL568 QYFSIPRYGF578 TALQHNEFLG588 QNFCPGLNAT 598 GNNPCNYATC608 TGEEYLVKQG618 IDLSPWGLWK628 NHVALACMIV638 IFLTIAYLKL 648 LFLKKY
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SER467
3.779
PHE470
4.623
LEU471
4.103
LEU474
4.952
MET515
4.986
TYR570
3.744
PHE571
4.248
TYR576
3.438
TRP624
4.466
LYS628
4.345
VAL631
4.755
|
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| PDB ID: 6HIJ Cryo-EM structure of the human ABCG2-MZ29-Fab complex with cholesterol and PE lipids docked | ||||||
| Method | Electron microscopy | Resolution | 3.56 Å | Mutation | No | [2] |
| PDB Sequence |
GAVLSFHNIC
43 YRVKLPVEKE62 ILSNINGIMK72 PGLNAILGPT82 GGGKSSLLDV92 LAARKDPSGL 102 SGDVLINGAP112 RPANFKCNSG122 YVVQDDVVMG132 TLTVRENLQF142 SAALRLATTM 152 TNHEKNERIN162 RVIQELGLDK172 VADSKVGTQF182 IRGVSGGERK192 RTSIGMELIT 202 DPSILFLDEP212 TTGLDSSTAN222 AVLLLLKRMS232 KQGRTIIFSI242 HQPRYSIFKL 252 FDSLTLLASG262 RLMFHGPAQE272 ALGYFESAGY282 HCEAYNNPAD292 FFLDIINGDL 328 IEKLAEIYVN338 SSFYKETKAE348 LHQLSGYTTS372 FCHQLRWVSK382 RSFKNLLGNP 392 QASIAQIIVT402 VVLGLVIGAI412 YFGLKNDSTG422 IQNRAGVLFF432 LTTNQCFSSV 442 SAVELFVVEK452 KLFIHEYISG462 YYRVSSYFLG472 KLLSDLLPMR482 MLPSIIFTCI 492 VYFMLGLKPK502 ADAFFVMMFT512 LMMVAYSASS522 MALAIAAGQS532 VVSVATLLMT 542 ICFVFMMIFS552 GLLVNLTTIA562 SWLSWLQYFS572 IPRYGFTALQ582 HNEFLGQNFC 592 PGLNATGNNP602 CNYATCTGEE612 YLVKQGIDLS622 PWGLWKNHVA632 LACMIVIFLT 642 IAYLKLLFLK652 KY
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ARG378
3.638
SER381
3.290
LYS382
4.022
PHE385
3.768
SER467
3.465
PHE470
4.042
LEU471
3.745
LEU474
4.133
LEU475
3.505
SER476
4.569
LEU479
3.862
PRO480
3.907
MET483
3.644
LEU484
1.489
ILE487
4.601
ASP504
3.744
PHE507
3.748
VAL508
4.053
MET510
3.686
PHE511
4.147
MET514
3.641
MET515
4.922
MET523
3.945
ALA526
3.996
ILE527
3.913
LEU540
4.799
CYS544
4.336
PHE547
3.421
MET548
3.646
PHE551
3.698
LEU568
3.379
TYR570
3.722
PHE571
3.531
SER572
4.500
TYR576
3.396
TRP624
3.984
TRP627
3.586
LYS628
4.500
VAL631
4.489
ALA632
3.938
ALA634
3.812
CYS635
3.626
MET636
4.488
ILE637
3.916
VAL638
3.941
ILE639
3.816
PHE640
3.653
LEU641
3.849
THR642
3.587
ILE643
3.979
TYR645
3.554
LYS647
2.852
|
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| PDB ID: 6VXI Structure of ABCG2 bound to mitoxantrone | ||||||
| Method | Electron microscopy | Resolution | 3.70 Å | Mutation | No | [3] |
| PDB Sequence |
AVLSFHNICY
44 RVKEILSNIN68 GIMKPGLNAI78 LGPTGGGKSS88 LLDVLAARKD98 PSGLSGDVLI 108 NGAPRPANFK118 CNSGYVVQDD128 VVMGTLTVRE138 NLQFSAALRL148 ATTMTNHEKN 158 ERINRVIQEL168 GLDKVADSKV178 GTQFIRGVSG188 GERKRTSIGM198 ELITDPSILF 208 LDEPTTGLDS218 STANAVLLLL228 KRMSKQGRTI238 IFSIHQPRYS248 IFKLFDSLTL 258 LASGRLMFHG268 PAQEALGYFE278 SAGYHCEAYN288 NPADFFLDII298 NGDLIEKLAE 334 IYVNSSFYKE344 TKAELHQLSG354 YTTSFCHQLR378 WVSKRSFKNL388 LGNPQASIAQ 398 IIVTVVLGLV408 IGAIYFGLKN418 DSTGIQNRAG428 VLFFLTTNQC438 FSSVSAVELF 448 VVEKKLFIHE458 YISGYYRVSS468 YFLGKLLSDL478 LPMRMLPSII488 FTCIVYFMLG 498 LKPKADAFFV508 MMFTLMMVAY518 SASSMALAIA528 AGQSVVSVAT538 LLMTICFVFM 548 MIFSGLLVNL558 TTIASWLSWL568 QYFSIPRYGF578 TALQHNEFLG588 QNFCPGLNAT 598 GNNPCNYATC608 TGEEYLVKQG618 IDLSPWGLWK628 NHVALACMIV638 IFLTIAYLKL 648 LFLKKY
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| PDB ID: 6VXH Structure of ABCG2 bound to imatinib | ||||||
| Method | Electron microscopy | Resolution | 4.00 Å | Mutation | No | [3] |
| PDB Sequence |
AVLSFHNICY
44 RVKEILSNIN68 GIMKPGLNAI78 LGPTGGGKSS88 LLDVLAARKD98 PSGLSGDVLI 108 NGAPRPANFK118 CNSGYVVQDD128 VVMGTLTVRE138 NLQFSAALRL148 ATTMTNHEKN 158 ERINRVIQEL168 GLDKVADSKV178 GTQFIRGVSG188 GERKRTSIGM198 ELITDPSILF 208 LDEPTTGLDS218 STANAVLLLL228 KRMSKQGRTI238 IFSIHQPRYS248 IFKLFDSLTL 258 LASGRLMFHG268 PAQEALGYFE278 SAGYHCEAYN288 NPADFFLDII298 NGDLIEKLAE 334 IYVNSSFYKE344 TKAELHQLSG354 TTSFCHQLRW379 VSKRSFKNLL389 GNPQASIAQI 399 IVTVVLGLVI409 GAIYFGLKND419 STGIQNRAGV429 LFFLTTNQCF439 SSVSAVELFV 449 VEKKLFIHEY459 ISGYYRVSSY469 FLGKLLSDLL479 PMRMLPSIIF489 TCIVYFMLGL 499 KPKADAFFVM509 MFTLMMVAYS519 ASSMALAIAA529 GQSVVSVATL539 LMTICFVFMM 549 IFSGLLVNLT559 TIASWLSWLQ569 YFSIPRYGFT579 ALQHNEFLGQ589 NFCPGLNATG 599 NNPCNYATCT609 GEEYLVKQGI619 DLSPWGLWKN629 HVALACMIVI639 FLTIAYLKLL 649 FLKKY
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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:570 or .A:571 or .A:576 or .A:624 or .A:628 or .A:631 or .A:632 or .A:635 or .A:636 or .A:639 or .A:640; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 6VXJ Structure of ABCG2 bound to SN38 | ||||||
| Method | Electron microscopy | Resolution | 4.10 Å | Mutation | No | [3] |
| PDB Sequence |
AVLSFHNICY
44 RVKEILSNIN68 GIMKPGLNAI78 LGPTGGGKSS88 LLDVLAARKD98 PSGLSGDVLI 108 NGAPRPANFK118 CNSGYVVQDD128 VVMGTLTVRE138 NLQFSAALRL148 ATTMTNHEKN 158 ERINRVIQEL168 GLDKVADSKV178 GTQFIRGVSG188 GERKRTSIGM198 ELITDPSILF 208 LDEPTTGLDS218 STANAVLLLL228 KRMSKQGRTI238 IFSIHQPRYS248 IFKLFDSLTL 258 LASGRLMFHG268 PAQEALGYFE278 SAGYHCEAYN288 NPADFFLDII298 NGDLIEKLAE 334 IYVNSSFYKE344 TKAELHQLSG354 YTTSFCHQLR378 WVSKRSFKNL388 LGNPQASIAQ 398 IIVTVVLGLV408 IGAIYFGLKN418 DSTGIQNRAG428 VLFFLTTNQC438 FSSVSAVELF 448 VVEKKLFIHE458 YISGYYRVSS468 YFLGKLLSDL478 LPMRMLPSII488 FTCIVYFMLG 498 LKPKADAFFV508 MMFTLMMVAY518 SASSMALAIA528 AGQSVVSVAT538 LLMTICFVFM 548 MIFSGLLVNL558 TTIASWLSWL568 QYFSIPRYGF578 TALQHNEFLG588 QNFCPGLNAT 598 GNNPCNYATC608 TGEEYLVKQG618 IDLSPWGLWK628 NHVALACMIV638 IFLTIAYLKL 648 LFLKKY
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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:570 or .A:571 or .A:576 or .A:628 or .A:632 or .A:635 or .A:636 or .A:639 or .A:640; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 7OJH ABCG2 topotecan turnover-1 state | ||||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | No | [4] |
| PDB Sequence |
GAVLSFHNIC
43 YRVVEKEILS65 NINGIMKPGL75 NAILGPTGGG85 KSSLLDVLAA95 RKDPSGLSGD 105 VLINGAPRPA115 NFKCNSGYVV125 QDDVVMGTLT135 VRENLQFSAA145 LRLATTMTNH 155 EKNERINRVI165 QELGLDKVAD175 SKVGTQFIRG185 VSGGERKRTS195 IGMELITDPS 205 ILFLDEPTTG215 LDSSTANAVL225 LLLKRMSKQG235 RTIIFSIHQP245 RYSIFKLFDS 255 LTLLASGRLM265 FHGPAQEALG275 YFESAGYHCE285 AYNNPADFFL295 DIINGDLIEK 331 LAEIYVNSSF341 YKETKAELHQ351 LSGYTTSFCH375 QLRWVSKRSF385 KNLLGNPQAS 395 IAQIIVTVVL405 GLVIGAIYFG415 LKNDSTGIQN425 RAGVLFFLTT435 NQCFSSVSAV 445 ELFVVEKKLF455 IHEYISGYYR465 VSSYFLGKLL475 SDLLPMRMLP485 SIIFTCIVYF 495 MLGLKPKADA505 FFVMMFTLMM515 VAYSASSMAL525 AIAAGQSVVS535 VATLLMTICF 545 VFMMIFSGLL555 VNLTTIASWL565 SWLQYFSIPR575 YGFTALQHNE585 FLGQNFCPGL 595 NATGNNPCNY605 ATCTGEEYLV615 KQGIDLSPWG625 LWKNHVALAC635 MIVIFLTIAY 645 LKLLFLKKY
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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 .B:570 or .B:571 or .B:576 or .B:624 or .B:628 or .B:631 or .B:632 or .B:635 or .B:636 or .B:639 or .B:640 or .B:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 7OJ8 ABCG2 E1S turnover-2 state | ||||||
| Method | Electron microscopy | Resolution | 3.40 Å | Mutation | No | [4] |
| PDB Sequence |
GAVLSFHNIC
43 YRVKLPVEKE62 ILSNINGIMK72 PGLNAILGPT82 GGGKSSLLDV92 LAARKDPSGL 102 SGDVLINGAP112 RPANFKCNSG122 YVVQDDVVMG132 TLTVRENLQF142 SAALRLATTM 152 TNHEKNERIN162 RVIQELGLDK172 VADSKVGTQF182 IRGVSGGERK192 RTSIGMELIT 202 DPSILFLDEP212 TTGLDSSTAN222 AVLLLLKRMS232 KQGRTIIFSI242 HQPRYSIFKL 252 FDSLTLLASG262 RLMFHGPAQE272 ALGYFESAGY282 HCEAYNNPAD292 FFLDIINGDK 326 PLIEKLAEIY336 VNSSFYKETK346 AELHQLSISY369 TTSFCHQLRW379 VSKRSFKNLL 389 GNPQASIAQI399 IVTVVLGLVI409 GAIYFGLKND419 STGIQNRAGV429 LFFLTTNQCF 439 SSVSAVELFV449 VEKKLFIHEY459 ISGYYRVSSY469 FLGKLLSDLL479 PMRMLPSIIF 489 TCIVYFMLGL499 KPKADAFFVM509 MFTLMMVAYS519 ASSMALAIAA529 GQSVVSVATL 539 LMTICFVFMM549 IFSGLLVNLT559 TIASWLSWLQ569 YFSIPRYGFT579 ALQHNEFLGQ 589 NFCPGLNATG599 NNPCNYATCT609 GEEYLVKQGI619 DLSPWGLWKN629 HVALACMIVI 639 FLTIAYLKLL649 FLKKY
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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:182 or .A:392 or .A:393 or .A:397 or .A:400 or .A:401 or .A:404 or .A:570 or .A:571 or .A:576 or .A:624 or .A:628 or .A:632 or .A:635 or .A:636 or .A:639 or .A:640 or .A:643; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 7OJI ABCG2 topotecan turnover-2 state | ||||||
| Method | Electron microscopy | Resolution | 3.40 Å | Mutation | No | [4] |
| PDB Sequence |
GAVLSFHNIC
43 YRVKPVEKEI63 LSNINGIMKP73 GLNAILGPTG83 GGKSSLLDVL93 AARKDPSGLS 103 GDVLINGAPR113 PANFKCNSGY123 VVQDDVVMGT133 LTVRENLQFS143 AALRLATTMT 153 NHEKNERINR163 VIQELGLDKV173 ADSKVGTQFI183 RGVSGGERKR193 TSIGMELITD 203 PSILFLDEPT213 TGLDSSTANA223 VLLLLKRMSK233 QGRTIIFSIH243 QPRYSIFKLF 253 DSLTLLASGR263 LMFHGPAQEA273 LGYFESAGYH283 CEAYNNPADF293 FLDIINGDKP 327 LIEKLAEIYV337 NSSFYKETKA347 ELHQLSYTTS372 FCHQLRWVSK382 RSFKNLLGNP 392 QASIAQIIVT402 VVLGLVIGAI412 YFGLKNDSTG422 IQNRAGVLFF432 LTTNQCFSSV 442 SAVELFVVEK452 KLFIHEYISG462 YYRVSSYFLG472 KLLSDLLPMR482 MLPSIIFTCI 492 VYFMLGLKPK502 ADAFFVMMFT512 LMMVAYSASS522 MALAIAAGQS532 VVSVATLLMT 542 ICFVFMMIFS552 GLLVNLTTIA562 SWLSWLQYFS572 IPRYGFTALQ582 HNEFLGQNFC 592 PGLNATGNNP602 CNYATCTGEE612 YLVKQGIDLS622 PWGLWKNHVA632 LACMIVIFLT 642 IAYLKLLFLK652 KY
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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:182 or .A:392 or .A:393 or .A:397 or .A:400 or .A:401 or .A:570 or .A:571 or .A:576 or .A:624 or .A:628 or .A:632 or .A:635 or .A:636 or .A:639 or .A:640 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural Basis of Drug Recognition by the Multidrug Transporter ABCG2. J Mol Biol. 2021 Jun 25;433(13):166980. | ||||
| REF 2 | Structural basis of small-molecule inhibition of human multidrug transporter ABCG2. Nat Struct Mol Biol. 2018 Apr;25(4):333-340. | ||||
| REF 3 | ABCG2 transports anticancer drugs via a closed-to-open switch. Nat Commun. 2020 May 8;11(1):2264. | ||||
| REF 4 | Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism. Nat Commun. 2021 Jul 19;12(1):4376. | ||||
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