3GST

STRUCTURE OF THE XENOBIOTIC SUBSTRATE BINDING SITE OF A GLUTATHIONE S-TRANSFERASE AS REVEALED BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PRODUCT COMPLEXES WITH THE DIASTEREOMERS OF 9-(S-GLUTATHIONYL)-10-HYDROXY-9, 10-DIHYDROPHENANTHRENE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d3gsta1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class mu GST	black rat (Rattus rattus ) [TaxId: 10117 ],	SCOPe (2.08)
A	d3gsta2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class mu GST	black rat (Rattus rattus ) [TaxId: 10117 ],	SCOPe (2.08)
B	d3gstb1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class mu GST	black rat (Rattus rattus ) [TaxId: 10117 ],	SCOPe (2.08)
B	d3gstb2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class mu GST	black rat (Rattus rattus ) [TaxId: 10117 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Thioredoxin-like	8044382	3000031	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GST C-terminal domain-like	8037522	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8044382	3000031	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GST C-terminal domain-like	8037522	3000305	SCOP2B (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	GST_C_3	e3gstA1	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_5	e3gstA2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
B	GST_C_3	e3gstB1	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_5	e3gstB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00043	Glutathione S-transferase, C-terminal domain (GST_C)	Glutathione S-transferase, C-terminal domain	GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins ...	GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain [1]. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes [2].	Domain
A, B	PF02798	Glutathione S-transferase, N-terminal domain (GST_N)	Glutathione S-transferase, N-terminal domain	Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity a ...	Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GLUTATHIONE S-TRANSFERASE	cation binding transition metal ion binding ion binding binding nickel cation binding metal ion binding small molecule binding amide binding modified amino acid binding oligopeptide binding anion binding glutathione binding sulfur compound binding glutathione transferase activity cation binding transition metal ion binding ion binding binding nickel cation binding metal ion binding small molecule binding amide binding modified amino acid binding oligopeptide binding anion binding glutathione binding sulfur compound binding glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity identical protein binding protein binding protein homodimerization activity protein dimerization activity kinase binding enzyme binding protein kinase binding organic cyclic compound binding steroid binding lipid binding	response to acid chemical response to stimulus response to chemical response to amino acid response to xenobiotic stimulus response to stress response to wounding response to axon injury multicellular organismal process system process sensory perception of chemical stimulus sensory perception nervous system process sensory perception of smell response to acid chemical response to stimulus response to chemical response to amino acid response to xenobiotic stimulus response to stress response to wounding response to axon injury multicellular organismal process system process sensory perception of chemical stimulus sensory perception nervous system process sensory perception of smell nitrobenzene metabolic process benzene-containing compound metabolic process metabolic process cellular process prostaglandin metabolic process icosanoid metabolic process fatty acid metabolic process unsaturated fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process prostanoid metabolic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process response to metal ion glutathione metabolic process modified amino acid metabolic process sulfur compound metabolic process amide metabolic process response to alcohol response to oxygen-containing compound response to ethanol response to lead ion cellular response to stimulus catabolic process cellular response to xenobiotic stimulus xenobiotic catabolic process xenobiotic metabolic process cellular response to chemical stimulus long-chain fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process long-chain fatty acid biosynthetic process hepoxilin metabolic process lipid biosynthetic process organic acid biosynthetic process fatty acid biosynthetic process carboxylic acid biosynthetic process hepoxilin biosynthetic process biosynthetic process sulfur compound biosynthetic process glutathione derivative biosynthetic process glutathione derivative metabolic process cellular detoxification of nitrogen compound cellular detoxification detoxification response to nitrogen compound detoxification of nitrogen compound response to toxic substance cellular response to stress cellular response to toxic substance	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004046	Glutathione S-transferase, C-terminal	Domain
A, B	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B	IPR050213	Glutathione S-transferase superfamily	Family
A, B	IPR003081	Glutathione S-transferase, Mu class	Family
A, B	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR036249	Thioredoxin-like superfamily	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 R01GM157729.