3wkt

X-ray diffraction
4.3Å resolution

Complex structure of an open form of NADPH-cytochrome P450 reductase and heme oxygenase-1

Released:

Function and Biology Details

Reactions catalysed:
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-132460 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NADPH--cytochrome P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 618 amino acids
Theoretical weight: 70.28 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00388 (Residues: 58-678; Coverage: 91%)
Gene name: Por
Sequence domains:
Heme oxygenase 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 267 amino acids
Theoretical weight: 30.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06762 (Residues: 1-267; Coverage: 92%)
Gene name: Hmox1
Sequence domains: Heme oxygenase

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand FMN 2 x FMN

Cofactor: Ligand NAP 2 x NAP

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P61
Unit cell:
a: 290.336Å b: 290.336Å c: 83.646Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.222 0.256
Expression system: Escherichia coli