› 4zvn

X-ray diffraction
1.87Å resolution

Reduced quinone reductase 2 in complex with acridine orange

Released:
DOI: 10.2210/pdb4zvn/pdb
PDB entry 4zvn coloured by chain, front view.
PDB entry 4zvn coloured by chain, side view.
PDB entry 4zvn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of DNA-Intercalating Agents to Oxidized and Reduced Quinone Reductase 2.
Leung KK, Shilton BH
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:
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: 230 amino acids
Theoretical weight: 25.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: 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:
Ligand ZN 3 x ZN
Ligand AO 2 x AO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 56.64Å b: 82.86Å c: 106.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.196
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

The diverse functionality of NQO1 and its roles in redox control.
Ross et al. (2021)
6 other articles