4Y23

Crystal structure of T399A precursor mutant protein of gamma-glutamyl transpeptidase from Bacillus licheniformis

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Gamma-glutamyltranspeptidase-like	8078199	4000420	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Class II glutamine amidotransferases	8078200	3000131	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01019	e4y23A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Gamma-glutamyltranspeptidase-like	F: PF01019	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01019	Gamma-glutamyltranspeptidase (G_glu_transpept)	Gamma-glutamyltranspeptidase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Gamma glutamyl transpeptidase,Gamma-glutamyltranspeptidase	peptidase activity omega peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity glutathione hydrolase activity aminoacyltransferase activity leukotriene C4 gamma-glutamyl transferase activity acyltransferase activity transferase activity	glutathione metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process amide biosynthetic process cellular modified amino acid metabolic process sulfur compound biosynthetic process organic substance metabolic process biosynthetic process peptide biosynthetic process cellular modified amino acid biosynthetic process glutathione biosynthetic process organic substance biosynthetic process glutathione metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process amide biosynthetic process cellular modified amino acid metabolic process sulfur compound biosynthetic process organic substance metabolic process biosynthetic process peptide biosynthetic process cellular modified amino acid biosynthetic process glutathione biosynthetic process organic substance biosynthetic process metabolic process sulfur compound metabolic process cellular process amide metabolic process nonribosomal peptide biosynthetic process peptide metabolic process organonitrogen compound catabolic process catabolic process cellular catabolic process sulfur compound catabolic process glutathione catabolic process organic substance catabolic process cellular modified amino acid catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A	IPR000101	Gamma-glutamyltranspeptidase	Family
A	IPR043137	Gamma-glutamyltranspeptidase, small subunit	Homologous Superfamily
A	IPR043138	Gamma-glutamyltranspeptidase, large subunit, C-terminal domain	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.