› 3tem

X-ray diffraction
1.45Å resolution

Quinone Oxidoreductase (NQ02) bound to the imidazoacridin-6-one 6a1

Released:
DOI: 10.2210/pdb3tem/pdb
PDB entry 3tem coloured by chain, front view.
PDB entry 3tem coloured by chain, side view.
PDB entry 3tem coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2): crystal structures, biochemical activity, and intracellular effects of imidazoacridin-6-ones.
Dunstan MS, Barnes J, Humphries M, Whitehead RC, Bryce RA, Leys D, Stratford IJ, Nolan KA
J Med Chem 54 6597-611 (2011)
PMID: 21859103

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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: 228 amino acids
Theoretical weight: 25.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16083 (Residues: 3-230; Coverage: 99%)
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:
Ligand ZN 2 x ZN
Ligand 6A1 2 x 6A1
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 56.764Å b: 83.571Å c: 106.281Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.165
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Acridine as an Anti-Tumour Agent: A Critical Review.
Varakumar et al. (2022)
4 other articles