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2NSM

Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0010815biological_processbradykinin catabolic process
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0046872molecular_functionmetal ion binding
A0051384biological_processresponse to glucocorticoid
Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeVkYvgNmHGnEaLGRelmlqL
ChainResidueDetails
APRO57-LEU79

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGGAVVAnYPY
ChainResidueDetails
AHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"17157876","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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