2BOA
Human procarboxypeptidase A4.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0042447 | biological_process | hormone catabolic process |
| A | 0043171 | biological_process | peptide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0042447 | biological_process | hormone catabolic process |
| B | 0043171 | biological_process | peptide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaVwLnaGiHSrEwISQataiwT |
| Chain | Residue | Details |
| A | PRO1060-THR1082 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
| Chain | Residue | Details |
| A | HIS1196-TYR1206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 |
| Chain | Residue | Details |
| A | GLU1270 | |
| B | GLU1270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2PCU |
| Chain | Residue | Details |
| A | PRO57 | |
| A | GLU1016 | |
| A | PHE1052 | |
| A | ARG1084 | |
| B | PRO57 | |
| B | GLU1016 | |
| B | PHE1052 | |
| B | ARG1084 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| A | VAL59 | |
| A | SER1136 | |
| B | VAL59 | |
| B | SER1136 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23746805, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| A | ASN1008 | |
| B | SER1014 | |
| B | LYS1085 | |
| B | ASP1158 | |
| A | TYR1012 | |
| A | HIS1013 | |
| A | SER1014 | |
| A | LYS1085 | |
| A | ASP1158 | |
| B | ASN1008 | |
| B | TYR1012 | |
| B | HIS1013 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:22294694, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4A94, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| A | HIS1069 | |
| A | GLU1072 | |
| A | HIS1196 | |
| B | HIS1069 | |
| B | GLU1072 | |
| B | HIS1196 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU |
| Chain | Residue | Details |
| A | ASN1148 | |
| B | ASN1148 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG1127 | |
| A | GLU1270 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| B | ARG1127 | |
| B | GLU1270 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG1127 | |
| A | ARG1071 | |
| A | GLU1270 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| B | ARG1127 | |
| B | ARG1071 | |
| B | GLU1270 |
