Function and Biology Details
Reaction catalysed:
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Flavoprotein pyridine nucleotide cytochrome reductase
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- Oxidoreductase FAD/NAD(P)-binding
- NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily
- FAD-binding domain, ferredoxin reductase-type
- Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding
- Riboflavin synthase-like beta-barrel
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
NADPH--cytochrome P450 reductase (preferred)
PDBe Complex ID:
PDB-CPX-147724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH--cytochrome P450 reductase
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 458 amino acids
Theoretical weight: 52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P16435 (Residues: 241-677; Coverage: 65%)
Sequence domains:
Structure domains:
