2PVG

Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase

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)
A	d2pvga1	Small proteins	Ferredoxin thioredoxin reductase (FTR), catalytic beta chain	Ferredoxin thioredoxin reductase (FTR), catalytic beta chain	Ferredoxin thioredoxin reductase (FTR), catalytic beta chain	Ferredoxin thioredoxin reductase (FTR), catalytic beta chain	(Synechocystis sp. ) [TaxId: 1143 ],	SCOPe (2.08)
A	d2pvga2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Synechocystis sp. ) [TaxId: 1143 ],	SCOPe (2.08)
B	d2pvgb_	All beta proteins	SH3-like barrel	Electron transport accessory proteins	Ferredoxin thioredoxin reductase (FTR), alpha (variable) chain	Ferredoxin thioredoxin reductase (FTR), alpha (variable) chain	(Synechocystis sp. ) [TaxId: 1143 ],	SCOPe (2.08)
C	d2pvgc_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	2Fe-2S ferredoxin	(Synechocystis sp. ) [TaxId: 1143 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ferredoxin thioredoxin reductase (FTR) catalytic beta chain	8036077	3001072	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Electron transport accessory proteins	8036078	3000325	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	2Fe-2S ferredoxin-like	8034049	3000113	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	PF02943	e2pvgA1	A: few secondary structure elements	X: Ferredoxin thioredoxin reductase (FTR), catalytic beta chain (From Topology)	H: Ferredoxin thioredoxin reductase (FTR), catalytic beta chain (From Topology)	T: Ferredoxin thioredoxin reductase (FTR), catalytic beta chain	F: PF02943	ECOD (1.6)
B	PF02941	e2pvgB1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF02941	ECOD (1.6)
C	PF00111	e2pvgC1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: PF00111	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.460.10	Alpha Beta	Alpha-Beta Complex	Ferredoxin Thioredoxin Reductase	Ferredoxin thioredoxin reductase catalytic beta subunit	CATH (4.3.0)
B	2.30.30.50	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
C	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02943	Ferredoxin thioredoxin reductase catalytic beta chain (FeThRed_B)	Ferredoxin thioredoxin reductase catalytic beta chain	-	Domain
B	PF02941	Ferredoxin thioredoxin reductase variable alpha chain (FeThRed_A)	Ferredoxin thioredoxin reductase variable alpha chain	-	Domain
C	PF00111	2Fe-2S iron-sulfur cluster binding domain (Fer2)	2Fe-2S iron-sulfur cluster binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Ferredoxin-thioredoxin reductase, catalytic chain	oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity ferredoxin-thioredoxin reductase activity oxidoreductase activity, acting on a sulfur group of donors, iron-sulfur protein as acceptor catalytic activity oxidoreductase activity, acting on iron-sulfur proteins as donors iron-sulfur cluster binding binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding electron transfer activity cation binding ion binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity ferredoxin-thioredoxin reductase activity oxidoreductase activity, acting on a sulfur group of donors, iron-sulfur protein as acceptor catalytic activity oxidoreductase activity, acting on iron-sulfur proteins as donors iron-sulfur cluster binding binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding electron transfer activity cation binding ion binding metal ion binding	photosynthesis cellular metabolic process metabolic process cellular process	-
B	Ferredoxin-thioredoxin reductase, variable chain	oxidoreductase activity catalytic activity	photosynthesis cellular metabolic process metabolic process cellular process	-
C	Ferredoxin-1	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding electron transfer activity cation binding ion binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036644	Ferredoxin thioredoxin reductase catalytic beta subunit superfamily	Homologous Superfamily
A	IPR024707	Ferredoxin-thioredoxin reductase catalytic subunit, cyanobacteria-type	Family
A	IPR004209	Ferredoxin thioredoxin reductase catalytic beta subunit	Family
B	IPR008990	Electron transport accessory-like domain superfamily	Homologous Superfamily
B	IPR044166	Ferredoxin-thioredoxin reductase, variable chain	Family
B	IPR004207	Ferredoxin thioredoxin reductase, alpha chain	Domain
C	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
C	IPR010241	Ferredoxin [2Fe-2S], plant	Family
C	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
C	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
C	IPR006058	2Fe-2S ferredoxin, iron-sulphur binding site	Binding 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.