1FNB

REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES

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
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1fnba1	All beta proteins	Reductase/isomerase/elongation factor common domain	Riboflavin synthase domain-like	Ferredoxin reductase FAD-binding domain-like	Ferredoxin reductase (flavodoxin reductase) N-terminal domain	spinach (Spinacia oleracea ) [TaxId: 3562 ],	SCOPe (2.08)
A	d1fnba2	Alpha and beta proteins (a/b)	Ferredoxin reductase-like, C-terminal NADP-linked domain	Ferredoxin reductase-like, C-terminal NADP-linked domain	Reductases	Ferredoxin reductase (flavodoxin reductase)	spinach (Spinacia oleracea ) [TaxId: 3562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Riboflavin synthase domain-like	8042045	3001812	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ferredoxin reductase-like, C-terminal NADP-linked domain	8044178	3001461	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	FAD_binding_1_1st	e1fnbA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: FAD_binding_1_1st	ECOD (1.6)
A	NAD_binding_1	e1fnbA2	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)
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)

Protein Family Annotation Pfam Database Homepage

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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	FERREDOXIN-NADP+ REDUCTASE	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 NADPH dehydrogenase activity oxidoreductase activity, acting on NAD(P)H	electron transport chain metabolic process cellular process generation of precursor metabolites and energy photosynthesis	membrane-bounded organelle intracellular anatomical structure plastid intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure plastid stroma organelle chloroplast stroma cytoplasm chloroplast chloroplast thylakoid membrane plastid membrane protein-containing complex membrane-bounded organelle intracellular anatomical structure plastid intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure plastid stroma organelle chloroplast stroma cytoplasm chloroplast chloroplast thylakoid membrane plastid membrane protein-containing complex membrane protein complex organelle outer membrane plastid thylakoid membrane plastid thylakoid organelle envelope bounding membrane of organelle membraneless organelle thylakoid plastid envelope membrane intracellular membraneless organelle thylakoid membrane chloroplast thylakoid membrane protein complex chloroplast thylakoid outer membrane photosynthetic membrane organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase	Domain
A	IPR001433	Oxidoreductase FAD/NAD(P)-binding	Domain
A	IPR035442	Ferredoxin--NADP reductase, plant and Cyanobacteria type	Family
A	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain	Homologous Superfamily
A	IPR017938	Riboflavin synthase-like beta-barrel	Homologous Superfamily
A	IPR017927	FAD-binding domain, ferredoxin reductase-type	Domain
A	IPR015701	Ferredoxin--NADP reductase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	ferredoxin--NADP reductase M-CSA #506	Ferredoxin reductase (FNR) catalyses the final electron transport step of linear photosynthesis, receiving one electron from two electron carrier ferredoxin proteins and uses these electrons to convert NADP+ into NADPH via hydride transfer from atom N(5) of the FAD cofactor using two molecules of ferredoxin (Fd) as the source of the electrons. In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin. FNR is a member of a large family of electron transport proteins containing NAD and FAD binding sites which form an FNR-like module.	Defined by 5 residues: TYR:A-95SER:A-96CYS:A-272GLU:A-312TYR:A-314 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.18.1.2 (PDB Primary Data) Search M-CSA Motif + EC 1.18.1.2

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.