1rwb

X-ray diffraction
2Å resolution

Cooperative Effect of Two Surface Amino Acid Mutations (Q252L and E170K) of Glucose Dehydrogenase from Bacillus megaterium IWG3 for the stabilization of Oligomeric State

Released:

Function and Biology Details

Reaction catalysed:
D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-154070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose 1-dehydrogenase Chains: A, B, E, F
Molecule details ›
Chains: A, B, E, F
Length: 261 amino acids
Theoretical weight: 28.1 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P40288 (Residues: 1-261; Coverage: 100%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2
Unit cell:
a: 118.5Å b: 65.4Å c: 118Å
α: 90° β: 92.6° γ: 90°
R-values:
R R work R free
0.224 0.224 0.267
Expression system: Escherichia coli