› 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:
DOI: 10.2210/pdb1qlh/pdb
PDB entry 1qlh coloured by chain, front view.
PDB entry 1qlh coloured by chain, side view.
PDB entry 1qlh coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer.
Ramaswamy S, Park DH, Plapp BV
Biochemistry 38 13951-9 (1999)
PMID: 10529241

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 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


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand ZN 2 x ZN
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

Quick links

Citations

5 review citations

Relating protein motion to catalysis.
Hammes-Schiffer et al. (2006)
4 more

4 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
3 more