› 1ped

X-ray diffraction
2.15Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent isopropanol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 351 amino acids
Theoretical weight: 37.76 KDa
Source organism: Clostridium beijerinckii
Expression system: Escherichia coli
UniProt:
  • Canonical: P25984 (Residues: 1-351; Coverage: 100%)
Gene name: adh
Sequence domains:
Structure domains:

Ligands and Environments

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: P212121
Unit cell:
a: 80.4Å b: 102.26Å c: 193.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.258
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Seeds to crystals.
Bergfors T. (2003)
1 more

2 mentions without citation

The conserved Glu-60 residue in Thermoanaerobacter brockii alcohol dehydrogenase is not essential for catalysis.
Kleifeld et al. (2003)
1 more