5OM9
Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with a thiirane mechanism-based inhibitor
Replaces: 4UF4Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue O2S A 401 |
| Chain | Residue |
| A | HIS69 |
| A | GLU270 |
| A | ZN402 |
| A | GLU72 |
| A | ARG127 |
| A | ASN144 |
| A | ARG145 |
| A | HIS196 |
| A | TYR248 |
| A | ALA250 |
| A | THR268 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | O2S401 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| B | HIS69 |
| B | GLU72 |
| B | HIS196 |
| B | O2S401 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 403 |
| Chain | Residue |
| A | GLU302 |
| A | HIS307 |
| B | GLU302 |
| B | HIS307 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide O2S B 401 and GLU B 270 |
| Chain | Residue |
| B | ARG-56 |
| B | HIS69 |
| B | GLU72 |
| B | ARG127 |
| B | ASN144 |
| B | ARG145 |
| B | HIS196 |
| B | SER197 |
| B | TYR198 |
| B | GLN200 |
| B | LEU201 |
| B | PHE238 |
| B | ILE243 |
| B | TYR248 |
| B | ALA250 |
| B | PHE269 |
| B | LEU271 |
| B | ZN402 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdtGiHSrEwVTQasgvwF |
| Chain | Residue | Details |
| A | PRO60-PHE82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 586 |
| Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
