3ai1

X-ray diffraction
2.38Å resolution

The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH and L-sorbose reveals the structure bases of its catalytic mechanism and high substrate selectivity

Released:

Function and Biology Details

Reaction catalysed:
D-glucitol + NADP(+) = L-sorbose + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-107393 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH-sorbose reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 28.35 KDa
Source organism: Gluconobacter frateurii
Expression system: Escherichia coli
UniProt:
  • Canonical: A4PB64 (Residues: 1-263; Coverage: 100%)
Gene name: sboA
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: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 124.186Å b: 124.124Å c: 60.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.261
Expression system: Escherichia coli