› 1n92

X-ray diffraction
1.47Å resolution

Horse Liver Alcohol Dehydrogenase Complexed with NAD+ and 4-Iodopyrazole

Released:
DOI: 10.2210/pdb1n92/pdb
Model geometry
Fit model/data
PDB entry 1n92 coloured by chain, front view.
PDB entry 1n92 coloured by chain, side view.
PDB entry 1n92 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase.
Rubach JK, Plapp BV
Biochemistry 42 2907-15 (2003)
PMID: 12627956

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: 39.85 KDa
Source organism: Equus caballus
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 PYZ 2 x PYZ
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 44.2Å b: 51.05Å c: 93.23Å
α: 78.96° β: 75.47° γ: 70.24°
R-values:
R R work R free
0.152 0.151 0.183

Quick links

Citations

3 review citations

FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism.
Krupenko SA. (2009)
2 more

2 mentions without citation

Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexes.
Plapp et al. (2012)
1 more