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4AZ3

crystal structure of cathepsin a, complexed with 15a

Functional Information from GO Data
ChainGOidnamespacecontents
A0004185molecular_functionserine-type carboxypeptidase activity
A0006508biological_processproteolysis
B0004185molecular_functionserine-type carboxypeptidase activity
B0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00131
Number of Residues8
DetailsCARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. LtGESYAG
ChainResidueDetails
ALEU146-GLY153

site_idPS00560
Number of Residues18
DetailsCARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. IafLtIkGAGHmVPtdkP
ChainResidueDetails
BILE419-PRO436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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