3gdf

X-ray diffraction
2.5Å resolution

Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.

Released:

Function and Biology Details

Reaction catalysed:
D-mannitol + NADP(+) = D-fructose + NADPH
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-142933 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent mannitol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 267 amino acids
Theoretical weight: 28.5 KDa
Source organism: Cladosporium herbarum
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0Y5 (Residues: 1-267; Coverage: 100%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 69.012Å b: 106.536Å c: 132.783Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.262
Expression system: Escherichia coli