1spx

X-ray diffraction
2.1Å resolution

Crystal Structure of Glucose Dehydrogenase of Caenorhabditis Elegans in the Apo-Form

Released:
Source organism: Caenorhabditis elegans
Entry authors: Schormann N, Zhou J, McCombs D, Bray T, Symersky J, Huang W-Y, Luan C-H, Gray R, Luo D, Arabashi A, Bunzel B, Nagy L, Lu S, Li S, Lin G, Zhang Y, Qiu S, Tsao J, Luo M, Carson M, Southeast Collaboratory for Structural Genomics (SECSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-172718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DeHydrogenases, Short chain Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 29.4 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q18946 (Residues: 1-278; Coverage: 100%)
Gene names: CELE_D1054.8, D1054.8
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 64.682Å b: 89.287Å c: 108.153Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.25
Expression system: Escherichia coli BL21(DE3)