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Alkohol Dehydrogenase
Exploring the Structure
Alcohol dehydrogenase uses two molecular "tools" to perform its reaction on ethanol. The first is a zinc atom, which is used to hold and position the alcoholic group on ethanol. The second is a large NAD cofactor (constructed using the vitamin niacin), which actually performs the reaction. PDB entry 1adc, shown here, contains ethanol molecules bound to the two active sites. A slightly-modified version of NAD was used in the structure analysis, so that the enzyme would not immediately attack the ethanol. Notice how the zinc atom, shown in light blue, is cradled by three amino acids from the protein: cysteine 46 to the left, cysteine 174 to the right, and histidine 67 above. The ethanol, shown in green and magenta, binds to the zinc and is positioned next to the NAD cofactor, which extends below the ethanol molecule in this illustration.
This illustration was created using RasMol. You can create similar illustrations by clicking on the PDB accession code above, and then selecting "View Structure."
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Last changed by: A.Honegger,