1GSF

GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
D	d1gsfd1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1gsfd2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1gsfa1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1gsfa2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1gsfb1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1gsfb2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gsfc1	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	Glutathione S-transferase (GST), C-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gsfc2	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione S-transferase (GST), N-terminal domain	Class alpha GST	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2B Superfamily	GST C-terminal domain-like	8042707	3000305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8042708	3000031	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioredoxin-like	8042708	3000031	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GST C-terminal domain-like	8042707	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GST C-terminal domain-like	8042707	3000305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8042708	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8042708	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GST C-terminal domain-like	8042707	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)
D	GST_C_3	e1gsfD1	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_5	e1gsfD2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
A	GST_C_3	e1gsfA1	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	e1gsfA2	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	e1gsfB1	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	e1gsfB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GST_N_5	ECOD (1.6)
C	GST_C_3	e1gsfC1	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_5	e1gsfC2	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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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, C, D	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, C, D	GLUTATHIONE TRANSFERASE A1-1	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor glutathione peroxidase activity catalytic activity fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor glutathione peroxidase activity catalytic activity fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups isomerase activity intramolecular oxidoreductase activity, transposing C=C bonds steroid delta-isomerase activity intramolecular oxidoreductase activity	cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus metabolic process cellular process xenobiotic metabolic process response to xenobiotic stimulus sulfur compound biosynthetic process biosynthetic process glutathione derivative biosynthetic process sulfur compound metabolic process glutathione derivative metabolic process cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus metabolic process cellular process xenobiotic metabolic process response to xenobiotic stimulus sulfur compound biosynthetic process biosynthetic process glutathione derivative biosynthetic process sulfur compound metabolic process glutathione derivative metabolic process fatty acid metabolic process long-chain fatty acid metabolic process unsaturated fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process linoleic acid metabolic process olefinic compound metabolic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process prostaglandin metabolic process icosanoid metabolic process prostanoid metabolic process developmental process epithelium development cellular developmental process cell differentiation anatomical structure development tissue development epithelial cell differentiation glutathione metabolic process modified amino acid metabolic process amide metabolic process	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR004046	Glutathione S-transferase, C-terminal	Domain
A, B, C, D	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A, B, C, D	IPR003080	Glutathione S-transferase, alpha class	Family
A, B, C, D	IPR004045	Glutathione S-transferase, N-terminal	Domain
A, B, C, D	IPR050213	Glutathione S-transferase superfamily	Family
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

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P08263	non-alcoholic fatty liver disease prostate cancer nephrosclerosis Nonalcoholic Steatohepatitis pancreatic intraductal papillary-mucinous neoplasm acute kidney failure schizophrenia adenoma breast cancer cystic fibrosis lung carcinoma myocardial ischemia pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia psoriasis non-alcoholic fatty liver disease prostate cancer nephrosclerosis Nonalcoholic Steatohepatitis pancreatic intraductal papillary-mucinous neoplasm acute kidney failure schizophrenia adenoma breast cancer cystic fibrosis lung carcinoma myocardial ischemia pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia psoriasis ulcerative colitis adrenal cortex carcinoma chronic obstructive pulmonary disease diabetes mellitus head and neck cancer malignant colon neoplasm nasopharyngeal carcinoma non-small cell lung carcinoma pancreatic intraductal papillary-mucinous carcinoma coronary artery disease malignant pancreatic neoplasm

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.