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 | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379 |
Chain | Residue | Details |
A | GLU270 | |
B | GLU270 | |
D | GLU270 | |
E | GLU270 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 |
Chain | Residue | Details |
A | HIS69 | |
E | HIS69 | |
E | GLU72 | |
E | HIS196 | |
A | GLU72 | |
A | HIS196 | |
B | HIS69 | |
B | GLU72 | |
B | HIS196 | |
D | HIS69 | |
D | GLU72 | |
D | HIS196 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 |
Chain | Residue | Details |
A | ARG127 | |
D | ASN144 | |
D | SER197 | |
D | TYR248 | |
E | ARG127 | |
E | ASN144 | |
E | SER197 | |
E | TYR248 | |
A | ASN144 | |
A | SER197 | |
A | TYR248 | |
B | ARG127 | |
B | ASN144 | |
B | SER197 | |
B | TYR248 | |
D | ARG127 |
Catalytic Information from CSA
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 |
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 |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 171 |
Chain | Residue | Details |
E | HIS69 | metal ligand |
E | GLU72 | metal ligand |
E | ARG127 | electrostatic stabiliser, hydrogen bond donor |
E | HIS196 | metal ligand |
E | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |