1ELM

CADMIUM-SUBSTITUTED BOVINE PACREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 5.5 AND 2 MM CHLORIDE IN MONOCLINIC CRYSTAL FORM.

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0004181	molecular_function	metallocarboxypeptidase activity
P	0006508	biological_process	proteolysis
P	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

Chain	Residue
P	HIS303

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
P	PRO60-PHE82

site_id	PS00133
Number of Residues	11
Details	CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY

Chain	Residue	Details
P	HIS196-TYR206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	293
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	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","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

Chain

Residue

Details