PDBe 4fgk

X-ray diffraction
1.4Å resolution

Oxidized quinone reductase 2 in complex with chloroquine

Released:

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: 233 amino acids
Theoretical weight: 26.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW 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
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P212121
Unit cell:
a: 56.37Å b: 83.11Å c: 106.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.132 0.174
Expression system: Escherichia coli BL21(DE3)