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X-ray diffraction
1.94Å resolution

N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb1nto/pdb
PDB entry 1nto coloured by chain, front view.
PDB entry 1nto coloured by chain, side view.
PDB entry 1nto coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity.
Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
FEBS Lett 539 14-8 (2003)
PMID: 12650918

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent alcohol dehydrogenase Chains: A, B, C, D, E, H
Molecule details ›
Chains: A, B, C, D, E, H
Length: 347 amino acids
Theoretical weight: 37.66 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: P39462 (Residues: 1-347; Coverage: 100%)
Gene names: SSO2536, adh
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 12 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2
Unit cell:
a: 215.327Å b: 91.594Å c: 118.238Å
α: 90° β: 99.2° γ: 90°
R-values:
R R work R free
0.214 0.21 0.244
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Characterization of a zinc-containing alcohol dehydrogenase with stereoselectivity from the hyperthermophilic archaeon Thermococcus guaymasensis.
Ying et al. (2011)
4 more

2 mentions without citation

Rapid catalytic template searching as an enzyme function prediction procedure.
Nilmeier et al. (2013)
1 more