2TPR

X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION

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)
B	d2tprb2	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	Trypanothione reductase, middle domain	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)
B	d2tprb1	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	Trypanothione reductase, N- and C-terminal domain	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)
B	d2tprb3	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	Trypanothione reductase	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)
A	d2tpra2	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	Trypanothione reductase, middle domain	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)
A	d2tpra1	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	Trypanothione reductase, N- and C-terminal domain	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)
A	d2tpra3	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	Trypanothione reductase	(Crithidia fasciculata ) [TaxId: 5656 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	GSR C-terminal domain-like	8056215	3000028	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin reductase-like	8056214	3000050	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GSR C-terminal domain-like	8056215	3000028	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioredoxin reductase-like	8056214	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)
B	Pyr_redox_dim	e2tprB1	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	e2tprB3	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	e2tprB2	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)
A	Pyr_redox_dim	e2tprA1	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	e2tprA3	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	e2tprA2	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)
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)
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, B	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, B	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	TRYPANOTHIONE REDUCTASE	flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity glutathione-disulfide reductase (NADPH) activity antioxidant activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule 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 trypanothione-disulfide reductase (NADPH) activity	cell redox homeostasis cellular homeostasis homeostatic process glutathione metabolic process modified amino acid metabolic process metabolic process cellular process sulfur compound metabolic process amide metabolic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cellular response to stress cell redox homeostasis cellular homeostasis homeostatic process glutathione metabolic process modified amino acid metabolic process metabolic process cellular process sulfur compound metabolic process amide 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 cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

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