6a2u

X-ray diffraction
2.6Å resolution

Crystal structure of gamma-alpha subunit complex from Burkholderia cepacia FAD glucose dehydrogenase

Released:

Function and Biology Details

Reaction catalysed:
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Twin-arginine translocation pathway signal Chains: A, C
Molecule details ›
Chains: A, C
Length: 121 amino acids
Theoretical weight: 13.05 KDa
Source organism: Burkholderia cepacia
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3KLY3 (Residues: 48-168; Coverage: 72%)
Gene name: BMULJ_04411
Glucose dehydrogenase Chains: B, D
Molecule details ›
Chains: B, D
Length: 545 amino acids
Theoretical weight: 60.74 KDa
Source organism: Burkholderia cepacia
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8GQE7 (Residues: 1-539; Coverage: 100%)
Gene name: gdhAlpha
Sequence domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P6522
Unit cell:
a: 110.521Å b: 110.521Å c: 524.877Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.204 0.261
Expression system: Escherichia coli BL21(DE3)