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5MRV

Crystal structure of human carboxypeptidase O in complex with NvCI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0098552cellular_componentside of membrane
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0098552cellular_componentside of membrane
C0004857molecular_functionenzyme inhibitor activity
C0008191molecular_functionmetalloendopeptidase inhibitor activity
C0010951biological_processnegative regulation of endopeptidase activity
C0030414molecular_functionpeptidase inhibitor activity
C0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. KiIwMdcGiHArEwIAPafcqwF
ChainResidueDetails
ALYS79-PHE101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues590
DetailsDomain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22294694","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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