› 5fa6

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH--cytochrome P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 618 amino acids
Theoretical weight: 70.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16435 (Residues: 64-677; Coverage: 91%)
Gene names: CYPOR, POR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand FMN 2 x FMN

Cofactor: Ligand NAP 2 x NAP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 70.073Å b: 119.322Å c: 156.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.28
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Human cytochrome P450 enzymes 5-51 as targets of drugs and natural and environmental compounds: mechanisms, induction, and inhibition - toxic effects and benefits.
Rendic et al. (2018)
5 other articles

9 mentions without citation

The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promiscuous Interactions With Structurally Diverse Redox Partners.
Esteves et al. (2020)
8 more