4J57 | pdb_00004j57

Structure of Plasmodium falciparum thioredoxin reductase-thioredoxin complex

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)
C [auth E]	d4j57e_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
D [auth F]	d4j57f_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth E]	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
D [auth F]	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	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	e4j57A4	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	e4j57A2	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	e4j57A5	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	e4j57B4	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	e4j57B2	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	e4j57B5	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 [auth E]	Thioredoxin	e4j57E1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
D [auth F]	Thioredoxin	e4j57F1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	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)
C [auth E]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
D [auth F]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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	PF00890	FAD binding domain (FAD_binding_2)	FAD binding domain	-	Family
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
C [auth E], D [auth F]	PF00085	Thioredoxin (Thioredoxin)	Thioredoxin	Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Thioredoxin reductase 2	thioredoxin-disulfide reductase (NADPH) activity protein-disulfide reductase [NAD(P)H] 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 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 protein-disulfide reductase [NAD(P)H] 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 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 anion binding nucleotide binding heterocyclic compound binding small molecule binding	cell redox homeostasis cellular homeostasis homeostatic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle
C [auth E], D [auth F]	Thioredoxin	oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity catalytic activity, acting on a protein protein-disulfide reductase activity catalytic activity	-	cellular anatomical structure intracellular anatomical structure cytoplasm 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	IPR023753	FAD/NAD(P)-binding domain	Domain
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	IPR006338	Thioredoxin/glutathione reductase selenoprotein	Family
A, B	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site	Active Site
C [auth E], D [auth F]	IPR017937	Thioredoxin, conserved site	Conserved Site
C [auth E], D [auth F]	IPR013766	Thioredoxin domain	Domain
C [auth E], D [auth F]	IPR005746	Thioredoxin	Family
C [auth E], D [auth F]	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.