7uut

X-ray diffraction
1.89Å resolution

Ternary complex crystal structure of secondary alcohol dehydrogenases from the Thermoanaerobacter ethanolicus mutants C295A and I86A provides better understanding of catalytic mechanism

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NADP-dependent isopropanol dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 352 amino acids
Theoretical weight: 37.65 KDa
Source organism: Thermoanaerobacter pseudethanolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P14941 (Residues: 1-352; Coverage: 100%)
Gene name: adh
Sequence domains:
NADP-dependent isopropanol dehydrogenase Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 352 amino acids
Theoretical weight: 37.68 KDa
Source organism: Thermoanaerobacter pseudethanolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P14941 (Residues: 1-352; Coverage: 100%)
Gene name: adh
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 79.87Å b: 124.56Å c: 166.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.231
Expression system: Escherichia coli