› 4fgl

X-ray diffraction
1.2Å resolution

Reduced quinone reductase 2 in complex with chloroquine

Released:
DOI: 10.2210/pdb4fgl/pdb
PDB entry 4fgl coloured by chain, front view.
PDB entry 4fgl coloured by chain, side view.
PDB entry 4fgl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of quinone reductase 2 bound to antimalarial drugs reveal conformational change upon reduction
Leung KK, Shilton BH
J. Biol. Chem. (2013)

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 233 amino acids
Theoretical weight: 26.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 4 x FAD
2 bound ligands:
Ligand ZN 4 x ZN
Ligand CLQ 5 x CLQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 54.31Å b: 105.71Å c: 82Å
α: 90° β: 90.17° γ: 90°
R-values:
R R work R free
0.16 0.159 0.174
Expression system: Escherichia coli BL21(DE3)

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