1H6V

Mammalian thioredoxin reductase

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	d1h6va2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d1h6va1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d1h6va3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d1h6vb2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d1h6vb1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d1h6vb3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d1h6ve2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d1h6ve1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d1h6ve3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d1h6vc2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d1h6vc1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d1h6vc3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d1h6vd2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d1h6vd1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d1h6vd3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d1h6vf2	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	Mammalian thioredoxin reductase, middle domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d1h6vf1	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	Mammalian thioredoxin reductase, N- and C-terminal domain	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d1h6vf3	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	Mammalian thioredoxin reductase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Glutathione reductase-like	8056198	4000121	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	GSR C-terminal domain-like	8056200	3000028	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GSR C-terminal domain-like	8056200	3000028	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GSR C-terminal domain-like	8056200	3000028	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GSR C-terminal domain-like	8056200	3000028	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GSR C-terminal domain-like	8056200	3000028	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioredoxin reductase-like	8056199	3000050	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	GSR C-terminal domain-like	8056200	3000028	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	e1h6vA1	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	e1h6vA3	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	e1h6vA2	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)
B	Pyr_redox_dim	e1h6vB1	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)
B	Pyr_redox_2_1	e1h6vB3	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)
B	Pyr_redox_2	e1h6vB2	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)
E	Pyr_redox_dim	e1h6vE1	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)
E	Pyr_redox_2_1	e1h6vE3	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)
E	Pyr_redox_2	e1h6vE2	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)
C	Pyr_redox_dim	e1h6vC1	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)
C	Pyr_redox_2_1	e1h6vC3	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)
C	Pyr_redox_2	e1h6vC2	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)
D	Pyr_redox_dim	e1h6vD1	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)
D	Pyr_redox_2_1	e1h6vD3	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)
D	Pyr_redox_2	e1h6vD2	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)
F	Pyr_redox_dim	e1h6vF1	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)
F	Pyr_redox_2_1	e1h6vF3	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)
F	Pyr_redox_2	e1h6vF2	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)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
E	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
E	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
D	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
D	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
F	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
F	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, B, C, D, E A, B, C, D, E, F	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, B, C, D, E A, B, C, D, E, F	PF00890	FAD binding domain (FAD_binding_2)	FAD binding domain	-	Family
A, B, C, D, E A, B, C, D, E, F	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, B, C, D, E A, B, C, D, E, F	THIOREDOXIN REDUCTASE	thioredoxin-disulfide reductase (NADPH) activity oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity disulfide oxidoreductase activity antioxidant activity catalytic activity, acting on a protein protein-disulfide reductase activity protein-disulfide reductase (NAD(P)H) activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding thioredoxin-disulfide reductase (NADPH) activity oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity disulfide oxidoreductase activity antioxidant activity catalytic activity, acting on a protein protein-disulfide reductase activity protein-disulfide reductase (NAD(P)H) activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding NAD(P)H oxidase H2O2-forming activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor selenate reductase activity cation binding transition metal ion binding mercury ion binding metal ion binding peroxidase activity oxidoreductase activity, acting on peroxide as acceptor NADPH peroxidase activity identical protein binding protein binding	response to stimulus response to chemical response to xenobiotic stimulus catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to stress response to wounding response to axon injury response to selenium ion cell population proliferation response to stimulus response to chemical response to xenobiotic stimulus catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to stress response to wounding response to axon injury response to selenium ion cell population proliferation developmental process multicellular organism development multicellular organismal process anatomical structure morphogenesis embryonic morphogenesis anatomical structure development embryo development gastrulation cellular response to stimulus cellular response to oxygen levels cellular response to hyperoxia cellular response to chemical stress cellular response to increased oxygen levels response to hyperoxia cellular response to chemical stimulus cellular response to stress response to oxygen levels response to abiotic stimulus response to increased oxygen levels regulation of biological process positive regulation of programmed cell death regulation of cellular process regulation of apoptotic process biological regulation positive regulation of biological process regulation of programmed cell death cell death positive regulation of apoptotic process apoptotic process programmed cell death positive regulation of cellular process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process NADPH oxidation phosphorus metabolic process pyridine nucleotide metabolic process response to copper ion cellular response to metal ion response to metal ion cellular response to copper ion benzene-containing compound metabolic process cell redox homeostasis cellular homeostasis homeostatic process halogen metabolic process serine family amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process selenocysteine metabolic process proteinogenic amino acid metabolic process response to oxidative stress cellular detoxification detoxification cellular oxidant detoxification cellular response to toxic substance response to toxic substance formation of primary germ layer mesoderm morphogenesis tissue development tissue morphogenesis anatomical structure formation involved in morphogenesis mesoderm formation mesoderm development	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol somatodendritic compartment cell body neuronal cell body nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I	Family
A, B, C, D, E A, B, C, D, E, F	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR006338	Thioredoxin/glutathione reductase selenoprotein	Family
A, B, C, D, E A, B, C, D, E, F	IPR046952	Glutathione reductase/thioredoxin reductase-like	Family
A, B, C, D, E A, B, C, D, E, F	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR023753	FAD/NAD(P)-binding domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site	Active Site

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.