2BGJ

X-Ray Structure of the Ferredoxin-NADP(H) Reductase from Rhodobacter capsulatus at 2.1 Angstroms

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d2bgjc1	All beta proteins	Reductase/isomerase/elongation factor common domain	Riboflavin synthase domain-like	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
C	d2bgjc2	Alpha and beta proteins (a/b)	Ferredoxin reductase-like, C-terminal NADP-linked domain	Ferredoxin reductase-like, C-terminal NADP-linked domain	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
D	d2bgjd1	All beta proteins	Reductase/isomerase/elongation factor common domain	Riboflavin synthase domain-like	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
D	d2bgjd2	Alpha and beta proteins (a/b)	Ferredoxin reductase-like, C-terminal NADP-linked domain	Ferredoxin reductase-like, C-terminal NADP-linked domain	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
A	d2bgja1	All beta proteins	Reductase/isomerase/elongation factor common domain	Riboflavin synthase domain-like	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
A	d2bgja2	Alpha and beta proteins (a/b)	Ferredoxin reductase-like, C-terminal NADP-linked domain	Ferredoxin reductase-like, C-terminal NADP-linked domain	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
B	d2bgjb1	All beta proteins	Reductase/isomerase/elongation factor common domain	Riboflavin synthase domain-like	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)
B	d2bgjb2	Alpha and beta proteins (a/b)	Ferredoxin reductase-like, C-terminal NADP-linked domain	Ferredoxin reductase-like, C-terminal NADP-linked domain	automated matches	automated matches	(Rhodobacter capsulatus ) [TaxId: 1061 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	FAD_binding_6	e2bgjC5	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: FAD_binding_6	ECOD (1.6)
C	NAD_binding_1	e2bgjC6	A: a/b three-layered sandwiches	X: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	H: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	T: Ferredoxin reductase-like, C-terminal NADP-linked domain	F: NAD_binding_1	ECOD (1.6)
D	FAD_binding_6	e2bgjD5	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: FAD_binding_6	ECOD (1.6)
D	NAD_binding_1	e2bgjD6	A: a/b three-layered sandwiches	X: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	H: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	T: Ferredoxin reductase-like, C-terminal NADP-linked domain	F: NAD_binding_1	ECOD (1.6)
A	FAD_binding_6	e2bgjA5	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: FAD_binding_6	ECOD (1.6)
A	NAD_binding_1	e2bgjA6	A: a/b three-layered sandwiches	X: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	H: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	T: Ferredoxin reductase-like, C-terminal NADP-linked domain	F: NAD_binding_1	ECOD (1.6)
B	FAD_binding_6	e2bgjB5	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: FAD_binding_6	ECOD (1.6)
B	NAD_binding_1	e2bgjB6	A: a/b three-layered sandwiches	X: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	H: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology)	T: Ferredoxin reductase-like, C-terminal NADP-linked domain	F: NAD_binding_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
C	3.40.50.80	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module	CATH (4.3.0)
D	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
D	3.40.50.80	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module	CATH (4.3.0)
A	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
A	3.40.50.80	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module	CATH (4.3.0)
B	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
B	3.40.50.80	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00175	Oxidoreductase NAD-binding domain (NAD_binding_1)	Oxidoreductase NAD-binding domain	Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.	Domain
A, B, C, D	PF00970	Oxidoreductase FAD-binding domain (FAD_binding_6)	Oxidoreductase FAD-binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	FERREDOXIN-NADP(H) REDUCTASE	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding ferredoxin-NAD(P) reductase activity oxidoreductase activity ferredoxin-NADP+ reductase activity oxidoreductase activity, acting on iron-sulfur proteins as donors oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor catalytic activity	pigment catabolic process pigment metabolic process heme metabolic process catabolic process tetrapyrrole metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process cellular process porphyrin-containing compound metabolic process tetrapyrrole catabolic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus pigment catabolic process pigment metabolic process heme metabolic process catabolic process tetrapyrrole metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process cellular process porphyrin-containing compound metabolic process tetrapyrrole catabolic 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	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase	Domain
A, B, C, D	IPR001433	Oxidoreductase FAD/NAD(P)-binding	Domain
A, B, C, D	IPR051930	Flavodoxin/Ferredoxin--NADP Reductase	Family
A, B, C, D	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain	Homologous Superfamily
A, B, C, D	IPR008333	Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain	Domain
A, B, C, D	IPR017938	Riboflavin synthase-like beta-barrel	Homologous Superfamily
A, B, C, D	IPR017927	FAD-binding domain, ferredoxin reductase-type	Domain
A, B, C, D	IPR033892	Ferredoxin--NADP reductase, bacteria	Family

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.