3GRT

HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX

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)
A	d3grta2	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD/NAD-linked reductases, N-terminal and central domains	Glutathione reductase, middle domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3grta1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD/NAD-linked reductases, N-terminal and central domains	Glutathione reductase, N- and C-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3grta3	Alpha and beta proteins (a+b)	CO dehydrogenase flavoprotein C-domain-like	FAD/NAD-linked reductases, dimerisation (C-terminal) domain	FAD/NAD-linked reductases, dimerisation (C-terminal) domain	Glutathione reductase	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)
A	SCOP2B Superfamily	GSR C-terminal domain-like	8056194	3000028	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioredoxin reductase-like	8001320	3000050	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	Pyr_redox_dim	e3grtA1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: Pyr_redox_dim	ECOD (1.6)
A	Pyr_redox_2_1	e3grtA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Pyr_redox_2_1	ECOD (1.6)
A	Pyr_redox_2	e3grtA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Pyr_redox_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00070	Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox)	Pyridine nucleotide-disulphide oxidoreductase	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.	Domain
A	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (Pyr_redox_dim)	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	GLUTATHIONE REDUCTASE	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding flavin adenine dinucleotide binding ion binding anion binding oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding flavin adenine dinucleotide binding ion binding anion binding oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity glutathione-disulfide reductase (NADPH) activity antioxidant activity glutathione disulfide oxidoreductase activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor electron transfer activity	cell redox homeostasis cellular homeostasis homeostatic process glutathione metabolic process cellular metabolic process metabolic process sulfur compound metabolic process cellular process amide metabolic process cellular modified amino acid metabolic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cell redox homeostasis cellular homeostasis homeostatic process glutathione metabolic process cellular metabolic process metabolic process sulfur compound metabolic process cellular process amide metabolic process cellular modified amino acid metabolic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cellular response to stress response to stress response to chemical cellular response to oxidative stress cellular response to chemical stress	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cell periphery cell surface membrane plasma membrane external side of plasma membrane side of membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cell periphery cell surface membrane plasma membrane external side of plasma membrane side of membrane extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytosol membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	Domain
A	IPR046952	Glutathione reductase/thioredoxin reductase-like	Family
A	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I	Family
A	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily	Homologous Superfamily
A	IPR006322	Glutathione reductase, eukaryote/bacterial	Family
A	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR023753	FAD/NAD(P)-binding domain	Domain
A	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site	Active Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P00390	amyotrophic lateral sclerosis hyperthyroidism Diabetes Mellitus, Experimental hemolytic anemia hypoglycemia contact dermatitis anemia plasma cell myeloma familial hemolytic anemia malignant glioma neurodegenerative disease non-small cell lung carcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia drug-induced liver injury Hodgkins lymphoma amyotrophic lateral sclerosis hyperthyroidism Diabetes Mellitus, Experimental hemolytic anemia hypoglycemia contact dermatitis anemia plasma cell myeloma familial hemolytic anemia malignant glioma neurodegenerative disease non-small cell lung carcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia drug-induced liver injury Hodgkins lymphoma invasive ductal breast carcinoma brain cancer pancreatic intraductal papillary-mucinous carcinoma parkinsonian disorder rheumatoid arthritis lung cancer myopathy autosomal recessive juvenile Parkinson disease 2 brain glioblastoma congenital anemia pancreatic intraductal papillary-mucinous 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.