PDBe 4zvk

X-ray diffraction
1.87Å resolution

Reduced quinone reductase 2 in complex with ethidium

Released:
Source organism: Homo sapiens
Primary publication:
Binding of DNA-Intercalating Agents to Oxidized and Reduced Quinone Reductase 2.
Biochemistry 54 7438-48 (2015)
PMID: 26636353

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 BL21(DE3)
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: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 57.02Å b: 82.57Å c: 106.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.198
Expression system: Escherichia coli BL21(DE3)