› 6oa7

X-ray diffraction
1.1Å resolution

Horse liver L57F alcohol dehydrogenase E complexed with NAD and trifluoroethanol

Released:
DOI: 10.2210/pdb6oa7/pdb
Model geometry
Fit model/data
PDB entry 6oa7 coloured by chain, front view.
PDB entry 6oa7 coloured by chain, side view.
PDB entry 6oa7 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer.
Kim K, Plapp BV
Biochemistry 59 862-879 (2020)
PMID: 31994873

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase E chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 39.89 KDa
Source organism: Equus caballus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00327 (Residues: 2-375; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAJ 2 x NAJ
3 bound ligands:
Ligand ZN 4 x ZN
Ligand ETF 2 x ETF
Ligand MRD 5 x MRD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P1
Unit cell:
a: 44.41Å b: 51.45Å c: 92.55Å
α: 91.9° β: 103.07° γ: 110.22°
R-values:
R R work R free
0.114 0.113 0.131
Expression system: Escherichia coli

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Citations

1 review citation

Metallated dihydropyridinates: prospects in hydride transfer and (electro)catalysis.
Parsons et al. (2023)
4 other articles