› 1qv7

X-ray diffraction
1.8Å resolution

HORSE LIVER ALCOHOL DEHYDROGENASE HIS51GLN/LYS228ARG MUTANT COMPLEXED WITH NAD+ AND 2,3-DIFLUOROBENZYL ALCOHOL

Released:
DOI: 10.2210/pdb1qv7/pdb
PDB entry 1qv7 coloured by chain, front view.
PDB entry 1qv7 coloured by chain, side view.
PDB entry 1qv7 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase.
LeBrun LA, Park DH, Ramaswamy S, Plapp BV
Biochemistry 43 3014-26 (2004)
PMID: 15023053

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure 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: 39.87 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 NAD 2 x NAD
2 bound ligands:
Ligand ZN 4 x ZN
Ligand DFB 2 x DFB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P1
Unit cell:
a: 44.05Å b: 50.962Å c: 92.466Å
α: 91.61° β: 103.03° γ: 109.86°
R-values:
R R work R free
0.178 0.177 0.222
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Conformational changes and catalysis by alcohol dehydrogenase.
Plapp BV. (2010)
2 more

1 mention without citation

Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase.
Plapp et al. (2021)