Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T98311 | Target Info | |||
| Target Name | HUMAN angiotensin-converting enzyme (ACE) | ||||
| Synonyms | Kininase II; Dipeptidyl carboxypeptidase I; DCP1; DCP; CD143 antigen; CD143; ACE | ||||
| Gene Name | SLC33A1 | ||||
| Biochemical Class | Glycosylase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Omapatrilat | Ligand Info | |||
| Canonical SMILES | C1CC(N2C(C1)SCCC(C2=O)NC(=O)C(CC3=CC=CC=C3)S)C(=O)O | ||||
| InChI | 1S/C19H24N2O4S2/c22-17(15(26)11-12-5-2-1-3-6-12)20-13-9-10-27-16-8-4-7-14(19(24)25)21(16)18(13)23/h1-3,5-6,13-16,26H,4,7-11H2,(H,20,22)(H,24,25)/t13-,14-,15-,16-/m0/s1 | ||||
| InChIKey | LVRLSYPNFFBYCZ-VGWMRTNUSA-N | ||||
| PubChem Compound ID | 656629 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6H5X Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex with Omapatrilat. | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [1] |
| PDB Sequence |
LDPGLQPGQF
10 SADEAGAQLF20 AQSYQSSAEQ30 VLFQSVAASW40 AHDTNITAEN50 ARRQEEAALL 60 SQEFAEAWGQ70 KAKELYEPIW80 QQFTDPQLRR90 IIGAVRTLGS100 ANLPLAKRQQ 110 YNALLSQMSR120 IYSTAKVCLP130 ATCWSLDPDL143 TNILASSRSY153 AMLLFAWEGW 163 HNAAGIPLKP173 LYEDFTALSN183 EAYKQDGFTD193 TGAYWRSWYN203 SPTFEDDLEH 213 LYQQLEPLYL223 NLHAFVRRAL233 HRRYGDRYIN243 LRGPIPAHLL253 GDMWAQSWEN 263 IYDMVVPFPD273 KPNLDVTSTM283 LQQGWQATHM293 FRVAEEFFTS303 LELSPMPPEF 313 WEGSMLEKPA323 DGREVVCHAS333 AWDFYNRKDF343 RIKQCTRVTM353 DQLSTVHHEM 363 GHIQYYLQYK373 DLPVSLRRGA383 NPGFHEAIGD393 VLALSVSTPE403 HLHKIGLLDR 413 VTNDTESDIN423 YLLKMALEKI433 AFLPFGYLVD443 QWRWGVFSGR453 TPPSRYNFDW 463 WYLRTKYQGI473 CPPVTRNETH483 FDAGAKFHVP493 NVTPYIRYFV503 SFVLQFQFHE 513 ALCKEAGYEG523 PLHQCDIYRS533 TKAGAKLRKV543 LRAGSSRPWQ553 EVLKDMVGLD 563 ALDAQPLLKY573 FQLVTQWLQE583 QNQQNGEVLG593 WPEYQWHPPL603 PDNYPEGI |
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|
|
GLN259
2.359
HIS331
1.924
ALA332
2.945
SER333
2.945
ALA334
3.600
THR358
3.395
HIS361
3.330
GLU362
3.084
HIS365
3.317
GLU389
3.273
ASP393
4.843
|
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| PDB ID: 6TT4 Crystal structure of 'Res_S2 mutant human Angiotensin-1 converting enzyme N-domain in complex with omapatrilat. | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [2] |
| PDB Sequence |
LDPGLQPGQF
10 SADEAGAQLF20 AQSYQSSAEQ30 VLFQSVAASW40 AHDTNITAEN50 ARRQEEAALL 60 SQEFAEAWGQ70 KAKELYEPIW80 QQFTDPQLRR90 IIGAVRTLGS100 ANLPLAKRQQ 110 YNALLSQMSR120 IYSTAKVCLP130 TCWSLDPDLT144 NILASSRSYA154 MLLFAWEGWH 164 NAAGIPLKPL174 YEDFTALSNE184 AYKQDGFTDT194 GAYWRSWYNS204 PTFEDDLEHL 214 YQQLEPLYLN224 LHAFVRRALH234 RRYGDRYINL244 RGPIPAHLLG254 DMWAQTWSNI 264 YDMVVPFPDK274 PNLDVTSTML284 QQGWQATHMF294 RVAEEFFTSL304 ELSPMPPEFW 314 EGSMLEKPAD324 GREVVCHASA334 WDFYNRKDFR344 IKQCTRVTME354 QLVVVHHEMG 364 HIQYFLQYKD374 LPVSLREGAN384 PGFHEAIGDV394 LALSVSTPEH404 LHKIGLLDRV 414 TNDTESDINY424 LLKMALDKIA434 FLPFGYLVDQ444 WRWGVFSGRT454 PPSRYNFDWW 464 YLRTKYQGIC474 PPVTRNETHF484 DAGAKFHVPN494 VTPYIRYFVS504 FVLQFQFHEA 514 LCKEAGYEGP524 LHQCDIYRST534 KAGAKLRKVL544 RAGSSRPWQE554 VLKDMVGLDA 564 LDAQPLLKYF574 QLVTQWLQEQ584 NQQNGEVLGW594 PEYQWHPPLP604 DNYP |
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|
|
GLN259
2.232
HIS331
2.052
ALA332
3.030
SER333
2.943
ALA334
3.641
VAL358
3.142
HIS361
3.307
GLU362
3.201
HIS365
3.249
GLU389
3.239
ASP393
4.992
|
|||||
| PDB ID: 6H5W Crystal structure of human Angiotensin-1 converting enzyme C-domain in complex with Omapatrilat. | ||||||
| Method | X-ray diffraction | Resolution | 1.37 Å | Mutation | Yes | [1] |
| PDB Sequence |
DEAEASKFVE
49 EYDRTSQVVW59 NEYAGANWNY69 NTNITTETSK79 ILLQKNMQIA89 QHTLKYGTQA 99 RKFDVNQLQN109 TTIKRIIKKV119 QDLERAALPA129 QELEEYNKIL139 LDMETTYSVA 149 TVCHPQGSCL159 QLEPDLTNVM169 ATSRKYEDLL179 WAWEGWRDKA189 GRAILQFYPK 199 YVELINQAAR209 LNGYVDAGDS219 WRSMYETPSL229 EQDLERLFQE239 LQPLYLNLHA 249 YVRRALHRHY259 GAQHINLEGP269 IPAHLLGNMW279 AQTWSNIYDL289 VVPFPSAPSM 299 DTTEAMLKQG309 WTPRRMFKEA319 DDFFTSLGLL329 PVPPEFWQKS339 MLEKPTDGRE 349 VVCHASAWDF359 YNGKDFRIKQ369 CTTVNLEDLV379 VAHHEMGHIQ389 YFMQYKDLPV 399 ALREGANPGF409 HEAIGDVLAL419 SVSTPKHLHS429 LNLLSSEGGS439 DEHDINFLMK 449 MALDKIAFIP459 FSYLVDQWRW469 RVFDGSITKE479 NYNQEWWSLR489 LKYQGLPPVP 500 RTQGDFDPGA510 KFHIPSSVPY520 IRYFVSFIIQ530 FQFHEALCQA540 AGHTGPLHKC 550 DIYQSKEAGQ560 RLATAMKLGF570 SRPWPEAMQL580 ITGQPQMSAS590 AMLSYFKPLL 600 DWLRTENELH610 GEKLGWPQYN620 WTPNS
|
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|
|
TRP59
4.674
TYR62
2.596
ASN66
1.957
ASN70
2.973
ASN85
2.330
ILE88
2.828
ALA89
4.961
LYS118
2.791
ASP121
2.719
GLU123
2.229
ARG124
2.113
LEU132
4.950
TYR135
2.583
ASN136
3.813
LEU139
3.129
GLU143
2.630
TYR213
3.879
SER219
2.335
TRP220
2.652
SER222
3.457
MET223
2.324
GLN281
2.397
THR282
4.899
HIS353
1.966
ALA354
2.101
SER355
2.673
ALA356
3.493
TRP357
3.143
TYR360
3.552
VAL380
2.609
HIS383
3.073
GLU384
2.409
HIS387
2.727
GLU403
2.377
PRO407
4.222
GLU411
3.236
ASP415
4.258
PHE457
2.650
PHE460
4.535
LYS511
1.893
PHE512
2.384
HIS513
2.488
SER516
2.960
SER517
3.770
VAL518
2.555
PRO519
2.443
TYR520
1.898
ARG522
1.947
TYR523
1.996
PHE527
2.911
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design. J Med Chem. 2018 Nov 21;61(22):10141-10154. | ||||
| REF 2 | ACE-domain selectivity extends beyond direct interacting residues at the active site. Biochem J. 2020 Apr 17;477(7):1241-1259. | ||||
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