5lbt

X-ray diffraction
1.75Å resolution

Structure of the human quinone reductase 2 (NQO2) in complex with imiquimod

Released:
Source organism: Homo sapiens
Entry authors: Schneider S, Gross O

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)
PDBe Complex ID:
PDB-CPX-147595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosyldihydronicotinamide dehydrogenase [quinone] Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 FAD 2 x FAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 57.689Å b: 80.925Å c: 106.198Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.227
Expression system: Escherichia coli BL21