1AYE
HUMAN PROCARBOXYPEPTIDASE A2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005773 | cellular_component | vacuole |
| A | 0006508 | biological_process | proteolysis |
| A | 0007039 | biological_process | protein catabolic process in the vacuole |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | HOH401 |
| site_id | S0 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| A | ARG145 |
| A | ASN144 |
| A | TYR248 |
| site_id | S1 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | ARG127 |
| A | GLU270 |
| site_id | S2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | ARG71 |
| A | SER197 |
| A | TYR198 |
| A | SER199 |
| site_id | S3 |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| A | PHE279 |
| site_id | S4 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| A | LYS122 |
| A | ARG124 |
| A | LYS128 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwLdaGiHArEwVTQatalwT |
| Chain | Residue | Details |
| A | PRO60-THR82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmFPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 95 |
| Details | Propeptide: {"description":"Activation peptide","featureId":"PRO_0000004353","evidences":[{"source":"PubMed","id":"8318831","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 292 |
| Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10742178","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9384570","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG127 | |
| A | GLU270 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG71 | |
| A | GLU270 | |
| A | ARG127 |
