1BAV
CARBOXYPEPTIDASE A COMPLEXED WITH 2-BENZYL-3-IODO-PROPANOIC ACID (BIP)
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 |
C | 0004181 | molecular_function | metallocarboxypeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008270 | molecular_function | zinc ion binding |
D | 0004181 | molecular_function | metallocarboxypeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 310 |
Chain | Residue |
A | HIS69 |
A | GLU72 |
A | HIS196 |
A | HOH398 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 310 |
Chain | Residue |
B | GLU72 |
B | HIS196 |
B | BIP311 |
B | HOH379 |
B | HIS69 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 310 |
Chain | Residue |
C | HIS69 |
C | GLU72 |
C | HIS196 |
C | BIP311 |
C | HOH391 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 310 |
Chain | Residue |
D | HIS69 |
D | GLU72 |
D | HIS196 |
D | HOH368 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BIP A 311 |
Chain | Residue |
A | HIS69 |
A | ASN144 |
A | ARG145 |
A | HIS196 |
A | LEU203 |
A | ILE243 |
A | ILE247 |
A | TYR248 |
A | GLU270 |
A | HOH359 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BIP B 311 |
Chain | Residue |
B | HIS69 |
B | ARG127 |
B | ASN144 |
B | ARG145 |
B | HIS196 |
B | ILE243 |
B | ALA250 |
B | THR268 |
B | GLU270 |
B | ZN310 |
B | HOH379 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BIP C 311 |
Chain | Residue |
C | HIS69 |
C | ASN144 |
C | ARG145 |
C | HIS196 |
C | ILE247 |
C | TYR248 |
C | THR268 |
C | GLU270 |
C | ZN310 |
C | HOH359 |
C | HOH391 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BIP D 311 |
Chain | Residue |
D | HIS69 |
D | ASN144 |
D | ARG145 |
D | HIS196 |
D | ILE243 |
D | TYR248 |
D | THR268 |
D | GLU270 |
D | HOH401 |
site_id | CTA |
Number of Residues | 1 |
Details | THE CATALYTIC ZN++ SITE. |
Chain | Residue |
A | ZN310 |
site_id | CTB |
Number of Residues | 1 |
Details | THE CATALYTIC ZN++ SITE. |
Chain | Residue |
B | ZN310 |
site_id | CTC |
Number of Residues | 1 |
Details | THE CATALYTIC ZN++ SITE. |
Chain | Residue |
C | ZN310 |
site_id | CTD |
Number of Residues | 1 |
Details | THE CATALYTIC ZN++ SITE. |
Chain | Residue |
D | ZN310 |
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 | |
C | GLU270 | |
D | 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 | |
A | GLU72 | |
D | HIS69 | |
D | GLU72 | |
D | HIS196 | |
A | HIS196 | |
B | HIS69 | |
B | GLU72 | |
B | HIS196 | |
C | HIS69 | |
C | GLU72 | |
C | 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 | |
C | ASN144 | |
C | SER197 | |
C | TYR248 | |
D | ARG127 | |
D | ASN144 | |
D | SER197 | |
D | TYR248 | |
A | ASN144 | |
A | SER197 | |
A | TYR248 | |
B | ARG127 | |
B | ASN144 | |
B | SER197 | |
B | TYR248 | |
C | 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 |
C | HIS69 | metal ligand |
C | GLU72 | metal ligand |
C | ARG127 | electrostatic stabiliser, hydrogen bond donor |
C | HIS196 | metal ligand |
C | 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 |
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 |