2PCU

Human carboxypeptidase A4 in complex with a cleaved hexapeptide.

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

Functional Information from PROSITE/UniProt

site_id	PS00132
Number of Residues	23
Details	CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaVwLnaGiHSrEwISQataiwT

Chain	Residue	Details
A	PRO60-THR82

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	294
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	1
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	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22294694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cbx

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1cbx