4AZ0

crystal structure of cathepsin a, complexed with 8a.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0006508	biological_process	proteolysis
B	0004185	molecular_function	serine-type carboxypeptidase activity
B	0006508	biological_process	proteolysis

Functional Information from PROSITE/UniProt

site_id	PS00131
Number of Residues	8
Details	CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. LtGESYAG

Chain	Residue	Details
A	LEU146-GLY153

---

site_id	PS00560
Number of Residues	18
Details	CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. IafLtIkGAGHmVPtdkP

Chain	Residue	Details
B	ILE419-PRO436

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PubMed","id":"8591035","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8591035","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8591035","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---