1HDU
Crystal structure of bovine pancreatic carboxypeptidase A complexed with aminocarbonylphenylalanine at 1.75 A
Functional 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 |
| D | 0004181 | molecular_function | metallocarboxypeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008270 | molecular_function | zinc ion binding |
| E | 0004181 | molecular_function | metallocarboxypeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1308 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | ING1309 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1308 |
| Chain | Residue |
| B | HIS69 |
| B | GLU72 |
| B | HIS196 |
| B | ING1309 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1308 |
| Chain | Residue |
| D | GLU72 |
| D | HIS196 |
| D | ING1309 |
| D | HIS69 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E1308 |
| Chain | Residue |
| E | HIS69 |
| E | GLU72 |
| E | HIS196 |
| E | ING1309 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ING A1309 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | ARG127 |
| A | ASN144 |
| A | ARG145 |
| A | HIS196 |
| A | SER197 |
| A | ILE243 |
| A | ILE247 |
| A | THR268 |
| A | GLU270 |
| A | ZN1308 |
| A | HOH2147 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ING B1309 |
| Chain | Residue |
| B | HIS69 |
| B | GLU72 |
| B | ARG127 |
| B | ASN144 |
| B | ARG145 |
| B | HIS196 |
| B | SER197 |
| B | ILE243 |
| B | TYR248 |
| B | THR268 |
| B | GLU270 |
| B | ZN1308 |
| B | HOH2144 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ING D1309 |
| Chain | Residue |
| D | HIS69 |
| D | GLU72 |
| D | ARG127 |
| D | ASN144 |
| D | ARG145 |
| D | HIS196 |
| D | SER197 |
| D | ILE243 |
| D | TYR248 |
| D | GLU270 |
| D | ZN1308 |
| D | HOH2149 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ING E1309 |
| Chain | Residue |
| E | HIS69 |
| E | GLU72 |
| E | ARG127 |
| E | ASN144 |
| E | ARG145 |
| E | HIS196 |
| E | SER197 |
| E | ILE243 |
| E | THR268 |
| E | GLU270 |
| E | ZN1308 |
| E | HOH2133 |
| E | HOH2150 |
| E | HOH2151 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF |
| Chain | Residue | Details |
| A | PRO60-PHE82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1172 |
| 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 | 4 |
| 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 | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]} |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| B | ARG127 | |
| B | GLU270 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| D | ARG127 | |
| D | GLU270 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| E | ARG127 | |
| E | GLU270 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG71 | |
| A | GLU270 | |
| A | ARG127 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| B | ARG71 | |
| B | GLU270 | |
| B | ARG127 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| D | ARG71 | |
| D | GLU270 | |
| D | ARG127 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| E | ARG71 | |
| E | GLU270 | |
| E | ARG127 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| A | HIS69 | metal ligand |
| A | GLU72 | metal ligand |
| A | ARG127 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS196 | metal ligand |
| A | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| B | HIS69 | metal ligand |
| B | GLU72 | metal ligand |
| B | ARG127 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS196 | metal ligand |
| B | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| D | HIS69 | metal ligand |
| D | GLU72 | metal ligand |
| D | ARG127 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS196 | metal ligand |
| D | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
