3QAG

Human Glutathione Transferase O2 with glutathione -new crystal form

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3qaga2	All alpha proteins	GST C-terminal domain-like	GST C-terminal domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3qaga1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	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	e3qagA1	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	e3qagA2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	Glutathione S-transferase omega-2	oxidoreductase activity catalytic activity oxidoreductase activity, acting on phosphorus or arsenic in donors, disulfide as acceptor methylarsonate reductase activity oxidoreductase activity, acting on phosphorus or arsenic in donors glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups identical protein binding protein binding binding oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity antioxidant activity oxidoreductase activity catalytic activity oxidoreductase activity, acting on phosphorus or arsenic in donors, disulfide as acceptor methylarsonate reductase activity oxidoreductase activity, acting on phosphorus or arsenic in donors glutathione transferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups identical protein binding protein binding binding oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity antioxidant activity glutathione disulfide oxidoreductase activity glutathione dehydrogenase (ascorbate) activity oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor	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 cellular response to arsenic-containing substance response to arsenic-containing substance monosaccharide metabolic process carbohydrate metabolic process oxoacid 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 cellular response to arsenic-containing substance response to arsenic-containing substance monosaccharide metabolic process carbohydrate metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process L-ascorbic acid metabolic process vitamin metabolic process lactone metabolic process small molecule metabolic process water-soluble vitamin metabolic process glutathione metabolic process modified amino acid metabolic process sulfur compound 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	IPR010987	Glutathione S-transferase, C-terminal-like	Domain
A	IPR004045	Glutathione S-transferase, N-terminal	Domain
A	IPR050983	Glutathione S-transferase Omega/HSP26	Family
A	IPR036282	Glutathione S-transferase, C-terminal domain superfamily	Homologous Superfamily
A	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A	IPR005442	Glutathione S-transferase, omega-class	Family
A	IPR040079	Glutathione transferase family	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9H4Y5	urinary bladder cancer astrocytic tumor cystic fibrosis invasive ductal breast carcinoma malignant ependymoma primitive neuroectodermal tumor atypical teratoid rhabdoid tumor glioblastoma large cell medulloblastoma malignant glioma Sjogren syndrome urinary bladder neoplasm breast cancer interstitial cystitis lung carcinoma urinary bladder cancer astrocytic tumor cystic fibrosis invasive ductal breast carcinoma malignant ependymoma primitive neuroectodermal tumor atypical teratoid rhabdoid tumor glioblastoma large cell medulloblastoma malignant glioma Sjogren syndrome urinary bladder neoplasm breast cancer interstitial cystitis lung carcinoma medulloblastoma spina bifida

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.