4CPA
REFINED CRYSTAL STRUCTURE OF THE POTATO INHIBITOR COMPLEX OF CARBOXYPEPTIDASE A AT 2.5 ANGSTROMS RESOLUTION
Replaces: 1CPAFunctional 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 |
I | 0004857 | molecular_function | enzyme inhibitor activity |
I | 0004866 | molecular_function | endopeptidase inhibitor activity |
J | 0004857 | molecular_function | enzyme inhibitor activity |
J | 0004866 | molecular_function | endopeptidase inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN I 308 |
Chain | Residue |
A | HIS69 |
A | GLU72 |
A | HIS196 |
I | VAL38 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN J 309 |
Chain | Residue |
B | HIS69 |
B | GLU72 |
B | HIS196 |
J | VAL38 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GLY A 308 |
Chain | Residue |
A | ASN144 |
A | ARG145 |
A | ILE247 |
A | TYR248 |
A | GLU270 |
I | VAL38 |
A | HIS69 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GLY B 308 |
Chain | Residue |
B | HIS69 |
B | ASN144 |
B | ARG145 |
B | ILE247 |
B | TYR248 |
B | GLU270 |
J | VAL38 |
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 | 2 |
Details | SITE: Interaction with carboxypeptidase |
Chain | Residue | Details |
I | VAL38 | |
J | VAL38 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1122280 |
Chain | Residue | Details |
I | GLX1 | |
J | GLX1 | |
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 | 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 | 3 |
Details | Annotated By Reference To The Literature 1cbx |
Chain | Residue | Details |
A | ARG71 | |
A | GLU270 | |
A | ARG127 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cbx |
Chain | Residue | Details |
B | ARG71 | |
B | GLU270 | |
B | 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 |