1bkj

X-ray diffraction
1.8Å resolution

NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI

Released:
Model geometry
Fit model/data
Data not deposited
Source organism: Vibrio harveyi
Primary publication:
Flavin reductase P: structure of a dimeric enzyme that reduces flavin.
Biochemistry 35 13531-9 (1996)
PMID: 8885832

Function and Biology Details

Reaction catalysed:
FMNH(2) + NADP(+) = FMN + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-176376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH-flavin oxidoreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 26.33 KDa
Source organism: Vibrio harveyi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56691 (Residues: 1-240; Coverage: 100%)
Gene name: frp
Sequence domains: Nitroreductase family
Structure domains: NADH Oxidase

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P21
Unit cell:
a: 51.2Å b: 85.9Å c: 58.1Å
α: 90° β: 109.3° γ: 90°
R-values:
R R work R free
0.175 0.175 0.207
Expression system: Escherichia coli