4qof

X-ray diffraction
1.55Å resolution

Crystal structure of fmn quinone reductase 2 AT 1.55A

Released:
Source organism: Homo sapiens
Entry authors: Serriere J, Boutin JA, Isabet T, Antoine M, Ferry G

Function and Biology Details

Reaction catalysed:
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a quinol
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosyldihydronicotinamide dehydrogenase [quinone] Chains: A, B
Molecule details ›
Chains: A, B
Length: 231 amino acids
Theoretical weight: 25.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16083 (Residues: 1-231; Coverage: 100%)
Gene names: NMOR2, NQO2
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 56.17Å b: 83.27Å c: 106.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.214 0.235
Expression system: Escherichia coli