Annotations: 3ITJ

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00070	e3itjA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF00070	ECOD (1.6)
A	PF07992	e3itjA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
B	PF00070	e3itjB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF00070	ECOD (1.6)
B	PF07992	e3itjB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
C	PF00070	e3itjC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF00070	ECOD (1.6)
C	PF07992	e3itjC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
D	PF00070	e3itjD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF00070	ECOD (1.6)
D	PF07992	e3itjD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	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)
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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Thioredoxin reductase 1	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 cation binding transition metal ion binding iron ion binding ion 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 cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding	cell redox homeostasis cellular homeostasis homeostatic process cellular response to stimulus response to stimulus cellular response to oxidative stress detoxification reactive oxygen species metabolic process cellular response to chemical stress response to superoxide cellular oxidant detoxification response to inorganic substance cellular response to oxygen radical cellular response to reactive oxygen species cell redox homeostasis cellular homeostasis homeostatic process cellular response to stimulus response to stimulus cellular response to oxidative stress detoxification reactive oxygen species metabolic process cellular response to chemical stress response to superoxide cellular oxidant detoxification response to inorganic substance cellular response to oxygen radical cellular response to reactive oxygen species cellular response to stress response to stress cellular detoxification cellular metabolic process response to oxygen-containing compound cellular response to oxygen-containing compound response to reactive oxygen species response to toxic substance removal of superoxide radicals superoxide metabolic process response to oxidative stress cellular response to chemical stimulus response to chemical cellular response to superoxide metabolic process cellular process cellular response to toxic substance response to oxygen radical	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle mitochondrion organelle intracellular membrane-bounded organelle mitochondrial intermembrane space membrane-enclosed lumen intracellular organelle lumen organelle envelope lumen organelle envelope intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle mitochondrion organelle intracellular membrane-bounded organelle mitochondrial intermembrane space membrane-enclosed lumen intracellular organelle lumen organelle envelope lumen organelle envelope organelle lumen mitochondrial envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR005982	Thioredoxin reductase	Family
A, B, C, D	IPR023753	FAD/NAD(P)-binding domain	Domain
A, B, C, D	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR008255	Pyridine nucleotide-disulphide oxidoreductase, class-II, 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 R01GM133198.