BAIT
ADH6
ADHVI, YMR318C
NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress
GO Process (3)
GO Function (3)
GO Component (0)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
ADH6
ADHVI, YMR318C
NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; protein abundance increases in response to DNA replication stress
GO Process (3)
GO Function (3)
GO Component (0)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Apo and Holo structures of an NADPH-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae.
The crystal structure of Saccharomyces cerevisiae ScAdh6p has been solved using the anomalous signal from the two zinc atoms found per subunit, and it constitutes the first structure determined from a member of the cinnamyl alcohol dehydrogenase family. ScAdh6p subunits exhibit the general fold of the medium-chain dehydrogenases/reductases (MDR) but with distinct specific characteristics. In the three crystal structures solved ... [more]
J. Mol. Biol. Aug. 20, 2004; 341(4);1049-62 [Pubmed: 15289102]
Throughput
- Low Throughput
Curated By
- BioGRID