4UEE
Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with the PHOSPHINIC INHIBITOR Acetyl-Leu-Ala-Y(PO2CH2)-homoPhe-OH
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE LA9 A 1309 |
Chain | Residue |
A | HIS69 |
A | TYR248 |
A | SER253 |
A | THR268 |
A | GLU270 |
A | PHE279 |
A | ZN1310 |
A | HOH2047 |
B | GLU163 |
A | ARG71 |
A | GLU72 |
A | ARG127 |
A | ASN144 |
A | ARG145 |
A | HIS196 |
A | TYR198 |
A | ILE243 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1310 |
Chain | Residue |
A | HIS69 |
A | GLU72 |
A | HIS196 |
A | LA91309 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE LA9 B 1309 |
Chain | Residue |
A | GLU163 |
B | HIS69 |
B | ARG71 |
B | GLU72 |
B | ARG127 |
B | ASN144 |
B | ARG145 |
B | HIS196 |
B | SER197 |
B | TYR198 |
B | ILE243 |
B | TYR248 |
B | THR268 |
B | GLU270 |
B | PHE279 |
B | ZN1310 |
B | HOH2050 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1310 |
Chain | Residue |
B | HIS69 |
B | GLU72 |
B | HIS196 |
B | LA91309 |
Functional Information from PROSITE/UniProt
site_id | PS00132 |
Number of Residues | 23 |
Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdtGiHSrEwVTQasgvwF |
Chain | Residue | Details |
A | PRO60-PHE82 |
site_id | PS00133 |
Number of Residues | 11 |
Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
Chain | Residue | Details |
A | HIS196-TYR206 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 586 |
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 | 2 |
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 | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V77","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |