2ABZ
Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase 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 |
C | 0004857 | molecular_function | enzyme inhibitor activity |
C | 0030414 | molecular_function | peptidase inhibitor activity |
D | 0004857 | molecular_function | enzyme inhibitor activity |
D | 0030414 | molecular_function | peptidase inhibitor activity |
E | 0004857 | molecular_function | enzyme inhibitor activity |
E | 0030414 | molecular_function | peptidase inhibitor activity |
F | 0004857 | molecular_function | enzyme inhibitor activity |
F | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1001 |
Chain | Residue |
A | HIS69 |
A | GLU72 |
A | HIS196 |
C | VAL66 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1002 |
Chain | Residue |
B | HIS69 |
B | GLU72 |
B | HIS196 |
E | VAL66 |
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 | SITE: Interaction with carboxypeptidase => ECO:0000250 |
Chain | Residue | Details |
C | VAL66 | |
D | VAL66 | |
E | VAL66 | |
F | VAL66 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 |
Chain | Residue | Details |
A | HIS69 | |
A | GLU72 | |
A | HIS196 | |
B | HIS69 | |
B | GLU72 | |
B | HIS196 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7 |
Chain | Residue | Details |
A | ARG127 | |
A | ASN144 | |
A | SER197 | |
A | TYR248 | |
B | ARG127 | |
B | ASN144 | |
B | SER197 | |
B | TYR248 |
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 |