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 | Cysteine Sulfenic Acid | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)N)SO | ||||
| InChI | 1S/C3H7NO3S/c4-2(1-8-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 | ||||
| InChIKey | FXIRVRPOOYSARH-REOHCLBHSA-N | ||||
| PubChem Compound ID | 165339 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 7Z70 Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with fosinoprilat | ||||||
| Method | X-ray diffraction | Resolution | 1.85 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 LNLLSSSDEH442 DINFLMKMAL 452 DKIAFIPFSY462 LVDQWRWRVF472 DGSITKENYN482 QEWWSLRLKY492 QGLPPVPRTQ 503 GDFDPGAKFH513 IPSSVPYIRY523 FVSFIIQFQF533 HEALCQAAGH543 TGPLHKCDIY 553 QSKEAGQRLA563 TAMKLGFSRP573 WPEAMQLITG583 QPQMSASAML593 SYFKPLLDWL 603 RTENELHGEK613 LGWP
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| 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 | [2] |
| 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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| PDB ID: 6F9T Crystal structure of human testis Angiotensin-1 converting enzyme in complex with Sampatrilat. | ||||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [3] |
| 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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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat. FEBS J. 2022 Nov;289(21):6659-6671. | ||||
| REF 2 | 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 3 | Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity. FEBS J. 2018 Apr;285(8):1477-1490. | ||||
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