5MRV

Crystal structure of human carboxypeptidase O in complex with NvCI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0005615	cellular_component	extracellular space
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016324	cellular_component	apical plasma membrane
A	0046872	molecular_function	metal ion binding
A	0098552	cellular_component	side of membrane
B	0004180	molecular_function	carboxypeptidase activity
B	0004181	molecular_function	metallocarboxypeptidase activity
B	0005615	cellular_component	extracellular space
B	0005886	cellular_component	plasma membrane
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0016324	cellular_component	apical plasma membrane
B	0046872	molecular_function	metal ion binding
B	0098552	cellular_component	side of membrane
C	0008191	molecular_function	metalloendopeptidase inhibitor activity
C	0010466	biological_process	negative regulation of peptidase activity
C	0010951	biological_process	negative regulation of endopeptidase activity
C	0030414	molecular_function	peptidase inhibitor activity
C	0046872	molecular_function	metal 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. KiIwMdcGiHArEwIAPafcqwF

Chain	Residue	Details
A	LYS79-PHE101

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01379

site_id	SWS_FT_FI3
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255