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	2
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:20088880

Chain	Residue	Details
B	THR403
D	THR403

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
B	THR421
D	THR421

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:20088880

Chain	Residue	Details
B	GLU423
B	GLU442
B	ASP445
D	GLU423
D	GLU442
D	ASP445

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:20088880, ECO:0007744|PDB:3A75

Chain	Residue	Details
B	SER464
B	GLY485
D	SER464
D	GLY485

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