› 2cdc

X-ray diffraction
1.5Å resolution

Sulfolobus solfataricus Glucose Dehydrogenase 1 in complex with NADP and Xylose

Released:
DOI: 10.2210/pdb2cdc/pdb
PDB entry 2cdc coloured by chain, front view.
PDB entry 2cdc coloured by chain, side view.
PDB entry 2cdc coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL
J Biol Chem 281 14796-804 (2006)
PMID: 16556607

Function and Biology Details

Reactions catalysed: 
D-galactose + NADP(+) = D-galactono-1,5-lactone + NADPH
An aldopyranose + NAD(P)(+) = an aldono-1,5-lactone + NAD(P)H 
D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H
D-galactose + NAD(+) = D-galactono-1,4-lactone + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131684 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose 1-dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 40.92 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O93715 (Residues: 1-366; Coverage: 100%)
Gene name: gdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
4 bound ligands:
Ligand XYS 6 x XYS
Ligand XYP 4 x XYP
Ligand ZN 8 x ZN
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 68.644Å b: 91.032Å c: 138.725Å
α: 90° β: 89.98° γ: 90°
R-values:
R R work R free
0.206 0.204 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
1 more

2 mentions without citation

Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.
Ren et al. (2022)
1 more