› 2nvb

X-ray diffraction
2.8Å resolution

Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)

Released:
DOI: 10.2210/pdb2nvb/pdb
PDB entry 2nvb coloured by chain, front view.
PDB entry 2nvb coloured by chain, side view.
PDB entry 2nvb coloured by chain, top view.
Source organism: Thermoanaerobacter brockii
Primary publication:
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.
Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y
Proteins 72 711-9 (2008)
PMID: 18260103

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147161 (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: 352 amino acids
Theoretical weight: 37.71 KDa
Source organism: Thermoanaerobacter brockii
Expression system: Escherichia coli
UniProt:
  • Canonical: P14941 (Residues: 1-352; Coverage: 100%)
Gene name: adh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 79.598Å b: 125.008Å c: 167.111Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.278
Expression system: Escherichia coli

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Citations

7 citation in other articles

Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.
Hawwa et al. (2009)
6 more

1 mention without citation

In Silico Discovery of Anticancer Peptides from Sanghuang.
Liu et al. (2022)