› 5kj6

X-ray diffraction
1.14Å resolution

V197I Horse liver alcohol dehydrogenase complexed with NAD+ and pentafluorobenzyl alcohol

Released:
DOI: 10.2210/pdb5kj6/pdb
PDB entry 5kj6 coloured by chain, front view.
PDB entry 5kj6 coloured by chain, side view.
PDB entry 5kj6 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis.
Shanmuganatham KK, Wallace RS, Ting-I Lee A, Plapp BV
Protein Sci 27 750-768 (2018)
PMID: 29271062

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: 39.87 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 NAJ 2 x NAJ
3 bound ligands:
Ligand ZN 4 x ZN
Ligand PFB 2 x PFB
Ligand MRD 4 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P1
Unit cell:
a: 44.47Å b: 51.65Å c: 92.68Å
α: 91.92° β: 103.01° γ: 110.17°
R-values:
R R work R free
0.137 0.136 0.164
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bicyclo[3.2.0]carbocyclic Molecules and Redox Biotransformations: The Evolution of Closed-Loop Artificial Linear Biocatalytic Cascades and Related Redox-Neutral Systems.
Willetts A. (2023)
2 other articles

1 mention without citation

Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis.
Shanmuganatham et al. (2018)