Crystal structure of Drosophila melanogaster alcohol dehydrogenase complexed with NADH and acetate at 1.6 A
The structure was published by Benach, J., Winberg, J.O., Svendsen, J.S., Atrian, S., Gonzalez-Duarte, R., and Ladenstein, R., in 2005 in a paper entitled "Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.63 Å and deposited in 2002.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of alcohol dehydrogenase.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: