› 1o2d

X-ray diffraction
1.3Å resolution

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 371 amino acids
Theoretical weight: 41.94 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X022 (Residues: 2-359; Coverage: 100%)
Gene name: TM_0920
Sequence domains: Iron-containing alcohol dehydrogenase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
2 bound ligands:
Ligand FE 2 x FE
Ligand TRS 2 x TRS
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 58.047Å b: 85.283Å c: 72.08Å
α: 90° β: 96.29° γ: 90°
R-values:
R R work R free
0.139 0.137 0.17
Expression system: Escherichia coli

Quick links

Citations

2 review citations

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals.
Jarboe LR. (2011)
1 more

13 mentions without citation

Mutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum.
Brown et al. (2011)
12 more