6OEZ

Crystal structure of Trypanothione Reductase from Trypanosoma brucei in complex with inhibitor (+)-N-(Cyclobutylmethyl)-3-{5-[1-(pyrrolidin-1-yl)cyclohexyl]-2-(1-{[(2S)-pyrro-lidin-2-yl]methyl}-1H-indol-5-yl)-1,3-thiazol-4-yl}prop-2-yn-1-amine

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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 [auth B]	Pyr_redox_dim	e6oezB2	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 [auth B]	Pyr_redox_2_1	e6oezB3	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 [auth B]	Pyr_redox_2	e6oezB1	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 [auth A]	Pyr_redox_dim	e6oezA1	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 [auth A]	Pyr_redox_2_1	e6oezA3	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 [auth A]	Pyr_redox_2	e6oezA2	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 [auth B]	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (utative)
A [auth B]	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (utative)
B [auth A]	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (utative)
B [auth A]	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth 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 [auth B], B [auth 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 [auth B], B [auth A]	Trypanothione 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 trypanothione-disulfide reductase (NADPH) activity cation binding metal ion binding	cell redox homeostasis cellular homeostasis homeostatic process	membrane-bounded organelle intracellular anatomical structure ciliary plasm cilium cellular anatomical entity cytoplasmic region plasma membrane bounded cell projection cytoplasm plasma membrane bounded cell projection cell projection organelle cytoplasm intracellular organelle peroxisome microbody membrane-bounded organelle intracellular anatomical structure ciliary plasm cilium cellular anatomical entity cytoplasmic region plasma membrane bounded cell projection cytoplasm plasma membrane bounded cell projection cell projection organelle cytoplasm intracellular organelle peroxisome microbody glycosome intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	Domain
A [auth B], B [auth A]	IPR046952	Glutathione reductase/thioredoxin reductase-like	Family
A [auth B], B [auth A]	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I	Family
A [auth B], B [auth A]	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR023753	FAD/NAD(P)-binding domain	Domain
A [auth B], B [auth A]	IPR001864	Trypanothione reductase	Family
A [auth B], B [auth A]	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.