› 1pl8

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reactions catalysed: 
L-iditol + NAD(+) = L-sorbose + NADH
(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH
Ribitol + NAD(+) = D-ribulose + NADH
Xylitol + NAD(+) = D-xylulose + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169473 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sorbitol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 356 amino acids
Theoretical weight: 38.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q00796 (Residues: 2-357; Coverage: 100%)
Gene name: SORD
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P62
Unit cell:
a: 133.776Å b: 133.776Å c: 224.708Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

8 mentions without citation

Detecting similar binding pockets to enable systems polypharmacology.
Duran-Frigola et al. (2017)
7 more