1E1L

STRUCTURE OF ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP obtained by cocrystallisation

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	d1e1la1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	C-terminal domain of adrenodoxin reductase-like	Adrenodoxin reductase of mitochondrial p450 systems	BOVINE (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d1e1la2	Alpha and beta proteins (a/b)	Nucleotide-binding domain	Nucleotide-binding domain	N-terminal domain of adrenodoxin reductase-like	Adrenodoxin reductase of mitochondrial p450 systems	BOVINE (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Thioredoxin reductase-like	8001453	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)
A	Pyr_redox_2_3	e1e1lA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Pyr_redox_2_3	ECOD (1.6)
A	NAD_binding_8	e1e1lA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Nucleotide-binding domain	F: NAD_binding_8	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ADRENODOXIN REDUCTASE	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding flavin adenine dinucleotide binding ion binding anion binding oxidoreductase activity NADPH-adrenodoxin reductase activity binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding flavin adenine dinucleotide binding ion binding anion binding oxidoreductase activity NADPH-adrenodoxin 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	electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process steroid metabolic process lipid biosynthetic process primary metabolic process steroid biosynthetic process lipid metabolic process organic hydroxy compound metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process steroid metabolic process lipid biosynthetic process primary metabolic process steroid biosynthetic process lipid metabolic process organic hydroxy compound metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process secondary alcohol metabolic process small molecule metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process NADPH oxidation phosphorus metabolic process pyridine nucleotide metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR023753	FAD/NAD(P)-binding domain	Domain
A	IPR050711	Electron transfer and nitrogen metabolism enzyme	Family
A	IPR021163	Ferredoxin-NADP+ reductase, adrenodoxin-type	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.