› 1piw

X-ray diffraction
3Å resolution

APO AND HOLO STRUCTURES OF AN NADP(H)-DEPENDENT CINNAMYL ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE

Released:
DOI: 10.2210/pdb1piw/pdb
PDB entry 1piw coloured by chain, front view.
PDB entry 1piw coloured by chain, side view.
PDB entry 1piw coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Apo and Holo structures of an NADPH-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae.
Valencia E, Larroy C, Ochoa WF, Parés X, Fita I, Biosca JA
J Mol Biol 341 1049-62 (2004)
PMID: 15289102

Function and Biology Details

Reaction catalysed: 
An alcohol + NADP(+) = an aldehyde + NADPH
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-170089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent alcohol dehydrogenase 6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 39.67 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q04894 (Residues: 1-360; Coverage: 100%)
Gene names: ADH6, YM9924.10C, YMR318C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 234.98Å b: 100.35Å c: 52.49Å
α: 90° β: 92.18° γ: 90°
R-values:
R R work R free
0.266 0.218 0.271
Expression system: Saccharomyces cerevisiae

Quick links

Citations

1 review citation

Functions of aldehyde reductases from Saccharomyces cerevisiae in detoxification of aldehyde inhibitors and their biotechnological applications.
Wang et al. (2018)
23 other articles

7 mentions without citation

A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.
Cahn et al. (2017)
6 more