3svl

X-ray diffraction
2.2Å resolution

Structural basis of the improvement of ChrR - a multi-purpose enzyme

Released:

Function and Biology Details

Reaction catalysed:
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Quinone reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 193 amino acids
Theoretical weight: 20.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGE6 (Residues: 1-188; Coverage: 100%)
Gene names: JW3691, b3713, chrR, yieF
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P6322
Unit cell:
a: 107.255Å b: 107.255Å c: 128.251Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.237 0.27
Expression system: Escherichia coli