6ZLB

Thioredoxin glutathione reductase from Schistosoma mansoni in complex with Indole-3-carbinol

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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	e6zlbA4	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	Glutaredoxin	e6zlbA3	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Glutaredoxin	ECOD (1.6)
A	Pyr_redox_2_1	e6zlbA1	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	e6zlbA2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF07992	Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2)	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	PF00462	Glutaredoxin (Glutaredoxin)	Glutaredoxin	-	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	Thioredoxin glutathione 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 flavin adenine dinucleotide binding binding nucleoside phosphate 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 flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding glutathione-disulfide reductase (NADPH) activity glutathione disulfide oxidoreductase activity cation binding metal ion binding	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 cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011899	Glutaredoxin, eukaryotic/virial	Domain
A	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	Domain
A	IPR011767	Glutaredoxin active site	Active Site
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	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR002109	Glutaredoxin	Domain
A	IPR023753	FAD/NAD(P)-binding domain	Domain
A	IPR006338	Thioredoxin/glutathione reductase selenoprotein	Family
A	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site	Active Site
A	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily

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.