3ai2

X-ray diffraction
1.9Å resolution

The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH

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, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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


Cofactor: Ligand NDP 8 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 124.29Å b: 60.98Å c: 124.45Å
α: 90° β: 89.99° γ: 90°
R-values:
R R work R free
0.175 0.172 0.221
Expression system: Escherichia coli