2V36

Crystal structure of gamma-glutamyl transferase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006751	biological_process	glutathione catabolic process
A	0036374	molecular_function	glutathione hydrolase activity
C	0006751	biological_process	glutathione catabolic process
C	0036374	molecular_function	glutathione hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00462
Number of Residues	25
Details	G_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfTVadrwGNvVSyTtTIEqlFG

Chain	Residue	Details
B	THR403-GLY427

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A75","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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