PDBe 1sg0

X-ray diffraction
1.5Å resolution

Crystal structure analysis of QR2 in complex with resveratrol

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of quinone reductase 2 in complex with resveratrol.
Biochemistry 43 11417-26 (2004)
PMID: 15350128

Function and Biology Details

Reaction catalysed:
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a quinol
Biochemical function:
Biological process:
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: 230 amino acids
Theoretical weight: 25.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P16083 (Residues: 2-231; Coverage: 100%)
Gene names: NMOR2, NQO2
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 83.33Å b: 106.372Å c: 56.982Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.214 0.234
Expression system: Escherichia coli