› 1q1n

X-ray diffraction
3.15Å resolution

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

Released:
DOI: 10.2210/pdb1q1n/pdb
PDB entry 1q1n coloured by chain, front view.
PDB entry 1q1n coloured by chain, side view.
PDB entry 1q1n 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 Chain: A
Molecule details ›
Chain: A
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

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3221
Unit cell:
a: 101.9Å b: 101.9Å c: 149.15Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.269 0.24 0.283
Expression system: Saccharomyces cerevisiae

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Citations

2 review citations

Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling.
Stomberski et al. (2019)
1 more

1 mention without citation

Design of a Microbial Remediation Inoculation Program for Petroleum Hydrocarbon Contaminated Sites Based on Degradation Pathways.
Li et al. (2021)