› 6o91

X-ray diffraction
1.1Å resolution

Horse liver L57F alcohol dehydrogenase complexed with NAD and pentafluorobenzyl alcohol

Released:
DOI: 10.2210/pdb6o91/pdb
PDB entry 6o91 coloured by chain, front view.
PDB entry 6o91 coloured by chain, side view.
PDB entry 6o91 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 PFB 2 x PFB
Ligand MRD 5 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P1
Unit cell:
a: 44.5Å b: 51.52Å c: 92.54Å
α: 91.8° β: 103.07° γ: 110.42°
R-values:
R R work R free
0.118 0.118 0.132
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.
Plapp et al. (2022)