8QVO

L211Q, L254N, T262G mutant of carboxypeptidase T from Thermoactinomyces vulgaris

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

Functional Information from PROSITE/UniProt

site_id	PS00132
Number of Residues	23
Details	CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeVlYtaLhHArEhLTVemalyT

Chain	Residue	Details
A	PRO60-THR82

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site_id	PS00133
Number of Residues	11
Details	CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HTYSELIqYPY

Chain	Residue	Details
A	HIS204-TYR214

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	304
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"},{"source":"PubMed","id":"1521526","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1521526","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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