PDBe 1xi2

X-ray diffraction
1.5Å resolution

Quinone Reductase 2 in Complex with Cancer Prodrug CB1954

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954.
Biochem. Biophys. Res. Commun. 336 332-8 (2005)
PMID: 16129418

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: 83.475Å b: 106.455Å c: 56.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.216 0.233
Expression system: Escherichia coli