2DBU

Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli

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. TTHySVvdkdGNaVAvTyTLNttFG

Chain	Residue	Details
B	THR391-GLY415

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:16618936, ECO:0000269|PubMed:18555071

Chain	Residue	Details
B	THR391
D	THR391

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:16618936

Chain	Residue	Details
B	THR409
B	ASN411
B	GLN430
B	ASP433
D	THR409
D	ASN411
D	GLN430
D	ASP433

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
B	SER462
B	GLY483
D	SER462
D	GLY483

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