4UEZ
Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with the PHOSPHINIC INHIBITOR Acetyl-Leu-Phe-Y(PO2CH2)-Phe-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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 420 |
Chain | Residue |
A | HIS179 |
A | GLU182 |
A | HIS306 |
A | LFF421 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE LFF A 421 |
Chain | Residue |
A | ARG255 |
A | GLU273 |
A | HIS306 |
A | SER307 |
A | TYR308 |
A | SER309 |
A | ILE353 |
A | ILE357 |
A | TYR358 |
A | ALA360 |
A | SER363 |
A | THR378 |
A | GLU380 |
A | PHE389 |
A | ZN420 |
A | HOH2045 |
B | GLU273 |
B | LFF421 |
A | HIS179 |
A | ARG181 |
A | GLU182 |
A | ARG237 |
A | ASN254 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 420 |
Chain | Residue |
B | HIS179 |
B | GLU182 |
B | HIS306 |
B | LFF421 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE LFF B 421 |
Chain | Residue |
A | GLU273 |
A | LFF421 |
B | HIS179 |
B | ARG181 |
B | GLU182 |
B | ARG237 |
B | ASN254 |
B | ARG255 |
B | THR274 |
B | HIS306 |
B | SER307 |
B | TYR308 |
B | SER309 |
B | ILE353 |
B | ILE357 |
B | TYR358 |
B | ALA360 |
B | SER363 |
B | THR378 |
B | GLU380 |
B | PHE389 |
B | ZN420 |
B | HOH2047 |
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 | PRO170-PHE192 |
site_id | PS00133 |
Number of Residues | 11 |
Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
Chain | Residue | Details |
A | HIS306-TYR316 |
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 |