Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T14705 | Target Info | |||
| Target Name | Bacterial Beta-glucuronidase (Bact uidA) | ||||
| Synonyms | GUS; Beta-D-glucuronoside glucuronosohydrolase | ||||
| Target Type | Preclinical Target | ||||
| Gene Name | Bact uidA | ||||
| Biochemical Class | Glycosyl hydrolase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: 2-[4-(1,3-Benzodioxol-5-Ylmethyl)piperazin-1-Yl]-N-[(1s,2s,5s)-2,5-Dimethoxycyclohexyl]acetamide | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-N-[(1S,2S,5S)-2,5-dimethoxycyclohexyl]acetamide | PDB:4JHZ | ||||
| Method | X-ray diffraction | Resolution | 2.83 Å | Mutation | No | [1] |
| PDB Sequence |
SHLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGVITD151 ENGKKKQSYF 161 HDFFNYAGIH171 RSVLYTTPNT182 WVDDITVVTH192 VAQDCNHASV202 DWQVVANGDV 212 SVELRDADQQ222 VVATGQGTSG232 TLQVVNPHLW242 QPGEGYLYEL252 CVTAKSQTEC 262 DIYPLRVGIR272 SVAVKGEQFL282 INHKPFYFTG292 FGRHEDADLR302 GKGFDNVLVH 313 DHALDWIGAN324 SYRTSHYPYA334 EELDWADEHG345 IVVIDETAAV355 GFNLSLNKPK 372 ELYSEEAVNG382 ETQQAHLQAI392 KELIARDKNH402 PSVVWSIANE413 PDTRPQGARE 423 YFAPLAEATR433 KLDPTRPITC443 VNVFCDAHTD454 TISDLFDVLC464 LNRYYGWYVQ 474 SGDLETAEKV484 LEKELLAWQE494 KLHQPIIITE504 YGVDTLAGLH514 SYTDWSEEYQ 526 CAWLDYHRVF537 DRVSAVVGEQ547 VWNFADFATS557 QGILRVGGNK567 KGIFTRDRKP 577 KSAAFLLQKR587 WTGNFGEKPQ598 QGG
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| Ligand Name: (2~{S},3~{S},4~{R},5~{R})-2-hexyl-4,5-bis(oxidanyl)piperidine-3-carboxylic acid | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-glucuronidase complex with C6-hexyl uronic isofagomine | PDB:6LEL | ||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [2] |
| PDB Sequence |
HMLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVMEHQG 109 GYTPFEADVT119 PYVIAGKSVR129 ITVCVNNELN139 WQTIPPGMVI149 TDENGKKKQS 159 YFHDFFNYAG169 IHRSVMLYTT179 PNTWVDDITV189 VTHVAQDCNH199 ASVDWQVANG 210 DVSVELRDAD220 QQVVATGQGT230 SGTLQVVNPH240 LWQPGEGYLY250 ELCVTAKSQT 260 ECDIYPLRVG270 IRSVAVKGEQ280 FLINHKPFYF290 TGFGRHEDAD300 LRGKGFDNVL 310 MVHDHALMDW320 IGANSYRTSH330 YPYAEEMLDW340 ADEHGIVVID350 ETAAVGFNLS 360 LGIGFENKPK372 ELYSEEAVNG382 ETQQAHLQAI392 KELIARDKNH402 PSVVMWSIAN 412 EPDTRPQGAR422 EYFAPLAEAT432 RKLDPTRPIT442 CVNVMFCDAH452 TDTISDLFDV 462 LCLNRYYGWY472 VQSGDLETAE482 KVLEKELLAW492 QEKLHQPIII502 TEYGVDTLAG 512 LHSMYTDMWS522 EEYQCAWLDM532 YHRVFDRVSA542 VVGEQVWNFA552 DFATSQGILR 562 VGGNKKGIFT572 RDRKPKSAAF582 LLQKRWTGMN592 FGEKPQQ
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| Ligand Name: (3S,4R,5R)-4,5-dihydroxypiperidine-3-carboxylic Acid | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-glucuronidase complex with uronic isofagomine | PDB:6LEG | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [2] |
| PDB Sequence |
HMLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVMEHQG 109 GYTPFEADVT119 PYVIAGKSVR129 ITVCVNNELN139 WQTIPPGMVI149 TDENGKKKQS 159 YFHDFFNYAG169 IHRSVMLYTT179 PNTWVDDITV189 VTHVAQDCNH199 ASVDWQVVAN 209 GDVSVELRDA219 DQQVVATGQG229 TSGTLQVVNP239 HLWQPGEGYL249 YELCVTAKSQ 259 TECDIYPLRV269 GIRSVAVKGE279 QFLINHKPFY289 FTGFGRHEDA299 DLRGKGFDNV 309 LMVHDHALMD319 WIGANSYRTS329 HYPYAEEMLD339 WADEHGIVVI349 DETAAVGFNL 359 SLGIGFEAGN369 KPKELYSEEA379 VNGETQQAHL389 QAIKELIARD399 KNHPSVVMWS 409 IANEPDTRPQ419 GAREYFAPLA429 EATRKLDPTR439 PITCVNVMFC449 DAHTDTISDL 459 FDVLCLNRYY469 GWYVQSGDLE479 TAEKVLEKEL489 LAWQEKLHQP499 IIITEYGVDT 509 LAGLHSMYTD519 MWSEEYQCAW529 LDMYHRVFDR539 VSAVVGEQVW549 NFADFATSQG 559 ILRVGGNKKG569 IFTRDRKPKS579 AAFLLQKRWT589 GMNFGEKPQQ599 GG |
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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 .SJ5 or .SJ52 or .SJ53 or :3SJ5;style chemicals stick;color identity;select .A:163 or .A:330 or .A:363 or .A:412 or .A:413 or .A:466 or .A:468 or .A:472 or .A:504 or .A:549 or .A:554 or .A:562 or .A:566 or .A:568; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 1-[(6,7-Dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl]-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea | PDB:3LPF | ||||
| Method | X-ray diffraction | Resolution | 2.26 Å | Mutation | No | [3] |
| PDB Sequence |
SHLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGVITD151 ENGKKKQSYF 161 HDFFNYAGIH171 RSVLYTTPNT182 WVDDITVVTH192 VAQDCNHASV202 DWQVVANGDV 212 SVELRDADQQ222 VVATGQGTSG232 TLQVVNPHLW242 QPGEGYLYEL252 CVTAKSQTEC 262 DIYPLRVGIR272 SVAVKGEQFL282 INHKPFYFTG292 FGRHEDADLR302 GKGFDNVLVH 313 DHALDWIGAN324 SYRTSHYPYA334 EELDWADEHG345 IVVIDETAAV355 GFNLSLGIGF 365 EAGNKPKELY375 SEEAVNGETQ385 QAHLQAIKEL395 IARDKNHPSV405 VWSIANEPDT 416 RPQGAREYFA426 PLAEATRKLD436 PTRPITCVNV446 FCDAHTDTIS457 DLFDVLCLNR 467 YYGWYVQSGD477 LETAEKVLEK487 ELLAWQEKLH497 QPIIITEYGV507 DTLAGLHSYT 518 DWSEEYQCAW529 LDYHRVFDRV540 SAVVGEQVWN550 FADFATSQGI560 LRVGGNKKGI 570 FTRDRKPKSA580 AFLLQKRWTG590 NFGEKPQQGG601
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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 .Z77 or .Z772 or .Z773 or :3Z77;style chemicals stick;color identity;select .A:162 or .A:163 or .A:360 or .A:361 or .A:362 or .A:363 or .A:413 or .A:446 or .A:448 or .A:468 or .A:472 or .A:473 or .A:504 or .A:556 or .A:557 or .A:561 or .A:562; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Selenomethionine | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea | PDB:3LPF | ||||
| Method | X-ray diffraction | Resolution | 2.26 Å | Mutation | No | [3] |
| PDB Sequence |
SHLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGVITD151 ENGKKKQSYF 161 HDFFNYAGIH171 RSVLYTTPNT182 WVDDITVVTH192 VAQDCNHASV202 DWQVVANGDV 212 SVELRDADQQ222 VVATGQGTSG232 TLQVVNPHLW242 QPGEGYLYEL252 CVTAKSQTEC 262 DIYPLRVGIR272 SVAVKGEQFL282 INHKPFYFTG292 FGRHEDADLR302 GKGFDNVLVH 313 DHALDWIGAN324 SYRTSHYPYA334 EELDWADEHG345 IVVIDETAAV355 GFNLSLGIGF 365 EAGNKPKELY375 SEEAVNGETQ385 QAHLQAIKEL395 IARDKNHPSV405 VWSIANEPDT 416 RPQGAREYFA426 PLAEATRKLD436 PTRPITCVNV446 FCDAHTDTIS457 DLFDVLCLNR 467 YYGWYVQSGD477 LETAEKVLEK487 ELLAWQEKLH497 QPIIITEYGV507 DTLAGLHSYT 518 DWSEEYQCAW529 LDYHRVFDRV540 SAVVGEQVWN550 FADFATSQGI560 LRVGGNKKGI 570 FTRDRKPKSA580 AFLLQKRWTG590 NFGEKPQQGG601
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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 .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:-1 or .A:0 or .A:2 or .A:3 or .A:4 or .A:11 or .A:12 or .A:13 or .A:14 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:95 or .A:96 or .A:97 or .A:103 or .A:104 or .A:106 or .A:107 or .A:113 or .A:114 or .A:115 or .A:116 or .A:138 or .A:139 or .A:140 or .A:145 or .A:146 or .A:148 or .A:149 or .A:157 or .A:158 or .A:159 or .A:160 or .A:161 or .A:173 or .A:174 or .A:176 or .A:177 or .A:185 or .A:186 or .A:281 or .A:289 or .A:291 or .A:292 or .A:293 or .A:295 or .A:297 or .A:306 or .A:307 or .A:308 or .A:309 or .A:310 or .A:312 or .A:313 or .A:314 or .A:315 or .A:316 or .A:317 or .A:319 or .A:320 or .A:321 or .A:322 or .A:323 or .A:325 or .A:326 or .A:333 or .A:334 or .A:335 or .A:336 or .A:338 or .A:339 or .A:340 or .A:341 or .A:348 or .A:349 or .A:350 or .A:359 or .A:369 or .A:370 or .A:371 or .A:397 or .A:398 or .A:400 or .A:405 or .A:406 or .A:408 or .A:409 or .A:439 or .A:440 or .A:441 or .A:442 or .A:445 or .A:446 or .A:448 or .A:449 or .A:450 or .A:462 or .A:464 or .A:466 or .A:467 or .A:468 or .A:469 or .A:470 or .A:471 or .A:472 or .A:475 or .A:476 or .A:478 or .A:481 or .A:482 or .A:485 or .A:488 or .A:501 or .A:508 or .A:514 or .A:515 or .A:517 or .A:518 or .A:519 or .A:521 or .A:522 or .A:525 or .A:528 or .A:529 or .A:530 or .A:531 or .A:533 or .A:534 or .A:535 or .A:536 or .A:551 or .A:586 or .A:587 or .A:588 or .A:589 or .A:590 or .A:592 or .A:593 or .A:594 or .A:595 or .A:597; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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SER-1
3.809
HIS0
1.327
LEU2
1.333
ARG3
4.380
PRO4
3.812
GLU11
4.170
ILE12
3.773
LYS13
3.263
LYS14
3.789
VAL85
3.668
LEU86
3.106
ARG87
2.691
PHE88
3.915
ASP89
3.097
GLY95
4.274
LYS96
3.541
VAL97
3.161
GLU103
3.841
VAL104
1.328
GLU106
1.321
HIS107
4.549
PRO113
3.844
PHE114
2.844
GLU115
2.694
ALA116
3.035
LEU138
3.730
ASN139
4.691
TRP140
3.175
PRO145
4.776
GLY146
1.320
VAL148
1.328
ILE149
3.864
LYS157
4.058
GLN158
3.452
SER159
2.901
TYR160
4.996
PHE161
2.815
SER173
4.104
VAL174
1.322
LEU176
1.324
TYR177
4.016
ASP185
4.150
ASP186
4.223
PHE281
4.372
TYR289
4.281
THR291
3.349
GLY292
4.923
PHE293
3.783
ARG295
3.478
GLU297
3.668
PHE306
3.772
ASP307
3.112
ASN308
3.268
VAL309
3.251
LEU310
1.317
VAL312
1.333
HIS313
3.234
ASP314
2.947
HIS315
3.057
ALA316
3.418
LEU317
1.323
ASP319
1.325
TRP320
3.393
ILE321
3.373
GLY322
3.110
ALA323
2.992
SER325
3.520
TYR326
3.172
TYR333
3.982
ALA334
2.647
GLU335
2.933
GLU336
1.329
LEU338
1.331
ASP339
3.553
TRP340
2.790
ALA341
3.101
VAL348
3.975
ILE349
3.798
ASP350
3.106
LEU359
4.470
ASN369
4.257
LYS370
3.993
PRO371
3.459
ALA397
3.901
ARG398
4.820
LYS400
4.940
VAL405
3.576
VAL406
1.324
TRP408
1.334
SER409
4.154
ARG439
4.105
PRO440
3.392
ILE441
3.888
THR442
3.866
ASN445
4.016
VAL446
1.318
PHE448
1.325
CYS449
2.758
ASP450
3.618
VAL462
3.283
CYS464
4.367
ASN466
3.540
ARG467
3.171
TYR468
3.161
TYR469
3.307
GLY470
4.313
TRP471
2.975
TYR472
4.819
SER475
3.534
GLY476
3.531
LEU478
4.363
ALA481
4.714
GLU482
2.969
LEU485
4.526
GLU488
4.487
ILE501
4.629
ASP508
3.561
HIS514
4.641
SER515
1.337
TYR517
1.329
THR518
3.241
ASP519
1.327
TRP521
1.313
SER522
3.332
TYR525
3.703
ALA528
2.940
TRP529
3.073
LEU530
3.324
ASP531
1.322
TYR533
1.322
HIS534
2.961
ARG535
2.869
VAL536
3.208
PHE551
3.578
LYS586
4.939
ARG587
3.085
TRP588
3.588
THR589
3.452
GLY590
1.329
ASN592
1.320
PHE593
3.469
GLY594
4.944
GLU595
4.217
PRO597
4.397
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: (2s,3r,4s,5r)-3,4,5-Trihydroxy-6-oxopiperidine-2-carboxylic acid | Ligand Info | |||||
| Structure Description | Crystal structure of E. coli beta-glucuronidase with the glucaro-d-lactam inhibitor bound | PDB:3K4D | ||||
| Method | X-ray diffraction | Resolution | 2.39 Å | Mutation | No | [3] |
| PDB Sequence |
SHMLRPVETP
8 TREIKKLDGL18 WAFSLDRENC28 GIDQRWWESA38 LQESRAIAVP48 GSFNDQFADA 58 DIRNYAGNVW68 YQREVFIPKG78 WAGQRIVLRF88 DAVTHYGKVW98 VNNQEVMEHQ 108 GGYTPFEADV118 TPYVIAGKSV128 RITVCVNNEL138 NWQTIPPGMV148 ITDENGKKKQ 158 SYFHDFFNYA168 GIHRSVMLYT178 TPNTWVDDIT188 VVTHVAQDCN198 HASVDWQVVA 208 NGDVSVELRD218 ADQQVVATGQ228 GTSGTLQVVN238 PHLWQPGEGY248 LYELCVTAKS 258 QTECDIYPLR268 VGIRSVAVKG278 EQFLINHKPF288 YFTGFGRHED298 ADLRGKGFDN 308 VLMVHDHALM318 DWIGANSYRT328 SHYPYAEEML338 DWADEHGIVV348 IDETAAVGFN 358 LSLGKPKELY375 SEEAVNGETQ385 QAHLQAIKEL395 IARDKNHPSV405 VMWSIANEPD 415 TRPQGAREYF425 APLAEATRKL435 DPTRPITCVN445 VMFCDAHTDT455 ISDLFDVLCL 465 NRYYGWYVQS475 GDLETAEKVL485 EKELLAWQEK495 LHQPIIITEY505 GVDTLAGLHS 515 MYTDMWSEEY525 QCAWLDMYHR535 VFDRVSAVVG545 EQVWNFADFA555 TSQGILRVGG 565 NKKGIFTRDR575 KPKSAAFLLQ585 KRWTGMNFGE595 KPQQGG
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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 .EVA or .EVA2 or .EVA3 or :3EVA;style chemicals stick;color identity;select .A:163 or .A:330 or .A:412 or .A:413 or .A:466 or .A:468 or .A:472 or .A:504 or .A:549 or .A:554 or .A:562 or .A:566 or .A:568; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 1-[(6,8-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl]-1-(2-Hydroxyethyl)-3-(4-Hydroxyphenyl)thiourea | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea | PDB:5CZK | ||||
| Method | X-ray diffraction | Resolution | 2.39 Å | Mutation | No | [4] |
| PDB Sequence |
SHLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGVITD151 ENGKKKQSYF 161 HDFFNYAGIH171 RSVLYTTPNT182 WVDDITVVTH192 VAQDCNHASV202 DWQVVANGDV 212 SVELRDADQQ222 VVATGQGTSG232 TLQVVNPHLW242 QPGEGYLYEL252 CVTAKSQTEC 262 DIYPLRVGIR272 SVAVKGEQFL282 INHKPFYFTG292 FGRHEDADLR302 GKGFDNVLVH 313 DHALDWIGAN324 SYRTSHYPYA334 EELDWADEHG345 IVVIDETAAV355 GFNLSLGIGF 365 NKPKELYSEE378 AVNGETQQAH388 LQAIKELIAR398 DKNHPSVVWS409 IANEPDTRPQ 419 GAREYFAPLA429 EATRKLDPTR439 PITCVNVFCD450 AHTDTISDLF460 DVLCLNRYYG 470 WYVQSGDLET480 AEKVLEKELL490 AWQEKLHQPI500 IITEYGVDTL510 AGLHSYTDWS 522 EEYQCAWLDY533 HRVFDRVSAV543 VGEQVWNFAD553 FATSQGILRV563 GGNKKGIFTR 573 DRKPKSAAFL583 LQKRWTGNFG594 EKPQQGG
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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 .57Z or .57Z2 or .57Z3 or :357Z;style chemicals stick;color identity;select .A:360 or .A:361 or .A:362 or .A:363 or .A:413 or .A:446 or .A:448 or .A:469 or .A:471 or .A:472 or .A:473 or .A:563; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 3-(2-Fluorophenyl)-1-(2-hydroxyethyl)-1-[(6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl]urea | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea | PDB:3LPG | ||||
| Method | X-ray diffraction | Resolution | 2.42 Å | Mutation | No | [3] |
| PDB Sequence |
SHLRPVETPT
9 REIKKLDGLW19 AFSLDRENCG29 IDQRWWESAL39 QESRAIAVPG49 SFNDQFADAD 59 IRNYAGNVWY69 QREVFIPKGW79 AGQRIVLRFD89 AVTHYGKVWV99 NNQEVEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGVITD151 ENGKKKQSYF 161 HDFFNYAGIH171 RSVLYTTPNT182 WVDDITVVTH192 VAQDCNHASV202 DWQVVANGDV 212 SVELRDADQQ222 VVATGQGTSG232 TLQVVNPHLW242 QPGEGYLYEL252 CVTAKSQTEC 262 DIYPLRVGIR272 SVAVKGEQFL282 INHKPFYFTG292 FGRHEDADLR302 GKGFDNVLVH 313 DHALDWIGAN324 SYRTSHYPYA334 EELDWADEHG345 IVVIDETAAV355 GFNLSLGIGF 365 EAGNKPKELY375 SEEAVNGETQ385 QAHLQAIKEL395 IARDKNHPSV405 VWSIANEPDT 416 RPQGAREYFA426 PLAEATRKLD436 PTRPITCVNV446 FCDAHTDTIS457 DLFDVLCLNR 467 YYGWYVQSGD477 LETAEKVLEK487 ELLAWQEKLH497 QPIIITEYGV507 DTLAGLHSYT 518 DWSEEYQCAW529 LDYHRVFDRV540 SAVVGEQVWN550 FADFATSQGI560 LRVGGNKKGI 570 FTRDRKPKSA580 AFLLQKRWTG590 NFGEKPQQGG601
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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 .Z78 or .Z782 or .Z783 or :3Z78;style chemicals stick;color identity;select .A:162 or .A:163 or .A:360 or .A:361 or .A:362 or .A:363 or .A:413 or .A:446 or .A:448 or .A:468 or .A:472 or .A:473 or .A:557 or .A:561 or .A:562; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: (2~{S},3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)-2-propyl-piperidine-3-carboxylic acid | Ligand Info | |||||
| Structure Description | Structure of E. coli beta-glucuronidase complex with C6-propyl uronic isofagomine | PDB:6LEJ | ||||
| Method | X-ray diffraction | Resolution | 2.62 Å | Mutation | No | [2] |
| PDB Sequence |
> Chain A
GSHMLRPVET 7 PTREIKKLDG17 LWAFSLDREN27 CGIDQRWWES37 ALQESRAIAV47 PGSFNDQFAD 57 ADIRNYAGNV67 WYQREVFIPK77 GWAGQRIVLR87 FDAVTHYGKV97 WVNNQEVMEH 107 QGGYTPFEAD117 VTPYVIAGKS127 VRITVCVNNE137 LNWQTIPPGM147 VITDENGKKK 157 QSYFHDFFNY167 AGIHRSVMLY177 TTPNTWVDDI187 TVVTHVAQDC197 NHASVDWQVV 207 ANGDVSVELR217 DADQQVVATG227 QGTSGTLQVV237 NPHLWQPGEG247 YLYELCVTAK 257 SQTECDIYPL267 RVGIRSVAVK277 GEQFLINHKP287 FYFTGFGRHE297 DADLRGKGFD 307 NVLMVHDHAL317 MDWIGANSYR327 TSHYPYAEEM337 LDWADEHGIV347 VIDETAAVGF 357 NLSLGIGFEN369 KPKELYSEEA379 VNGETQQAHL389 QAIKELIARD399 KNHPSVVMWS 409 IANEPDTRPQ419 GAREYFAPLA429 EATRKLDPTR439 PITCVNVMFC449 DAHTDTISDL 459 FDVLCLNRYY469 GWYVQSGDLE479 TAEKVLEKEL489 LAWQEKLHQP499 IIITEYGVDT 509 LAGLHSMYTD519 MWSEEYQCAW529 LDMYHRVFDR539 VSAVVGEQVW549 NFADFATSQG 559 ILRVGGNKKG569 IFTRDRKPKS579 AAFLLQKRWT589 GMNFGEKPQQ599 > Chain B MLRPVETPTR 10 EIKKLDGLWA20 FSLDRENCGI30 DQRWWESALQ40 ESRAIAVPGS50 FNDQFADADI 60 RNYAGNVWYQ70 REVFIPKGWA80 GQRIVLRFDA90 VTHYGKVWVN100 NQEVMEHQGG 110 YTPFEADVTP120 YVIAGKSVRI130 TVCVNNELNW140 QTIPPGMVIT150 DENGKKKQSY 160 FHDFFNYAGI170 HRSVMLYTTP180 NTWVDDITVV190 THVAQASVDW204 QVVANGDVSV 214 ELRDADQQVV224 ATGQGTSGTL234 QVVGEGYLYE251 LCVTAKSQTE261 CDIYPLRVGI 271 RSVAVKGEQF281 LINHKPFYFT291 GFGRHEDADL301 RGKGFDNVLM311 VHDHALMDWI 321 GANSYRTSHY331 PYAEEMLDWA341 DEHGIVVIDE351 TAAVGFNLSL361 GIGFENKPKE 373 LYSEEAVNGE383 TQQAHLQAIK393 ELIARDKNHP403 SVVMWSIANE413 PDTRPQGARE 423 YFAPLAEATR433 KLDPTRPITC443 VNVMFCDAHT453 DTISDLFDVL463 CLNRYYGWYV 473 QSGDLETAEK483 VLEKELLAWQ493 EKLHQPIIIT503 EYGVDTLAGL513 HSMYTDMWSE 523 EYQCAWLDMY533 HRVFDRVSAV543 VGEQVWNFAD553 FATSQGILRV563 GGNKKGIFTR 573 DRKPKSAAFL583 LQKRWTGMNF593 GEKPQQG
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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 .CKX or .CKX2 or .CKX3 or :3CKX;style chemicals stick;color identity;select .A:163 or .A:330 or .A:361 or .A:412 or .A:413 or .A:446 or .A:447 or .A:448 or .A:466 or .A:468 or .A:472 or .A:504 or .A:549 or .A:554 or .A:562 or .A:566 or .A:568 or .B:163 or .B:330 or .B:361 or .B:412 or .B:413 or .B:447 or .B:448 or .B:466 or .B:468 or .B:472 or .B:504 or .B:549 or .B:554 or .B:562 or .B:566 or .B:568; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP163[A]
2.835
HIS330[A]
2.480
LEU361[A]
4.225
ASN412[A]
4.107
GLU413[A]
2.810
VAL446[A]
4.906
MET447[A]
4.433
PHE448[A]
4.376
ASN466[A]
4.386
TYR468[A]
3.530
TYR472[A]
2.796
GLU504[A]
2.713
TRP549[A]
2.876
PHE554[A]
3.943
ARG562[A]
3.618
ASN566[A]
3.188
LYS568[A]
2.746
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Molecular insights into microbial beta-glucuronidase inhibition to abrogate CPT-11 toxicity. Mol Pharmacol. 2013 Aug;84(2):208-17. | ||||
| REF 2 | Entropy-driven binding of gut bacterial Beta-glucuronidase inhibitors ameliorates irinotecan-induced toxicity. Commun Biol. 2021 Mar 4;4(1):280. | ||||
| REF 3 | Alleviating cancer drug toxicity by inhibiting a bacterial enzyme. Science. 2010 Nov 5;330(6005):831-5. | ||||
| REF 4 | Structure and Inhibition of Microbiome beta-Glucuronidases Essential to the Alleviation of Cancer Drug Toxicity. Chem Biol. 2015 Sep 17;22(9):1238-49. | ||||
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