X-ray diffraction
2.19Å resolution

Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH


Function and Biology Details

Reaction catalysed:
Propan-2-ol + NADP(+) = acetone + NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
NADP-dependent isopropanol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 352 amino acids
Theoretical weight: 37.85 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: P25984 (Residues: 166-253, 255-301; Coverage: 39%)
  • Canonical: P14941 (Residues: 1-165, 254-254, 302-352; Coverage: 62%)
Gene name: adh
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 79.376Å b: 83.003Å c: 119.691Å
α: 90° β: 99.93° γ: 90°
R R work R free
0.166 0.165 0.228
Expression system: Escherichia coli