› 4fr2

X-ray diffraction
3.2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 43.48 KDa
Source organism: Oenococcus oeni ATCC BAA-1163
Expression system: Escherichia coli
UniProt:
  • Canonical: A0NIJ1 (Residues: 2-390; Coverage: 100%)
Gene names: OENOO_49030, dhaT
Sequence domains: Iron-containing alcohol dehydrogenase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P43212
Unit cell:
a: 88.825Å b: 88.825Å c: 151.028Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.281 0.279 0.334
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Extreme makeover: Engineering the activity of a thermostable alcohol dehydrogenase (AdhD) from Pyrococcus furiosus.
Solanki et al. (2016)
9 other articles

3 mentions without citation

Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase.
Carbone et al. (2015)
2 more