3NIV

The crystal structure of Glutathione S-transferase from Legionella pneumophila

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3niva2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
A	d3niva1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
B	d3nivb2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
B	d3nivb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
B	d3nivb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
C	d3nivc2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
C	d3nivc1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
C	d3nivc3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
D	d3nivd2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
D	d3nivd1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)
D	d3nivd3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Legionella pneumophila subsp. pneumophila str. Philadelphia 1 ) [TaxId: 272624 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	GST_C_3	e3nivA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
A	GST_N	e3nivA5	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
B	GST_C_3	e3nivB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
B	GST_N	e3nivB5	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
C	GST_C_3	e3nivC4	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
C	GST_N	e3nivC3	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)
D	GST_C_3	e3nivD4	A: alpha superhelices	X: Repetitive alpha hairpins	H: Glutathione S-transferase (GST)-C (From Topology)	T: Glutathione S-transferase (GST)-C	F: GST_C_3	ECOD (1.6)
D	GST_N	e3nivD3	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
A	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)
C	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
C	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)
D	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
D	1.20.1050.10	Mainly Alpha	Up-down Bundle	Glutathione S-transferase Yfyf (Class Pi)	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13417	Glutathione S-transferase, N-terminal domain (GST_N_3)	Glutathione S-transferase, N-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Glutathione S-transferase	glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity isomerase activity maleylacetoacetate isomerase activity cis-trans isomerase activity	catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process cellular metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process L-phenylalanine metabolic process proteinogenic amino acid metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process glutathione metabolic process sulfur compound metabolic process amide metabolic process cellular modified amino acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR034330	Glutathione S-transferases, class Zeta , C-terminal	Domain
A, B, C, D	IPR005955	Glutathione S-transferases, class Zeta	Family
A, B, C, D	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B, C, D	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B, C, D	IPR034333	Glutathione S-transferases, class Zeta , N-terminal	Domain
A, B, C, D	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, B, C, D	IPR040079	Glutathione transferase family	Family

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 R01GM157729.