7EQZ

Crystal structure of Carboxypeptidase B complexed with Potato Carboxypeptidase Inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0006508	biological_process	proteolysis
A	0008270	molecular_function	zinc ion binding
I	0004866	molecular_function	endopeptidase inhibitor activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	290
Details	Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34658092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34750241","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7EQZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Interaction with carboxypeptidase"}

Chain

Residue

Details

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