PDBe 1qlh

X-ray diffraction
2.07Å resolution

HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR

Released:

Function and Biology Details

Reaction catalysed:
(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase E chain Chain: A
Molecule details ›
Chain: A
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2221
Unit cell:
a: 55.07Å b: 73.72Å c: 180.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.254
Expression system: Escherichia coli