The Three Side Chain Active Site of Alcohol Dehydrogenase



Picture created using PyMol and PDB file 1HTB

The active site of alcohol dehydrogenase is composed of the side chains of the amino acids histidine and cysteine.  Specifically, they are the residues Histidine-67, Cysteine-46, and Cysteine-174.  It also contains two zinc ions that hold the hydroxyl group of the alcohol in place, as well as an NAD cofactor which actually causes the reaction.  Since the enzyme consists of two polypeptides, alcohol dehydrogenase is a dimer and has two active sites.



activesitenew
Picture made using PyMol and PDB file 1HTB

Active site of alcohol dehydrogenase (yellow) showing the two zinc ions (red) and the NAD cofactor (orange).






wholeenzyme
Picture made using PyMol and PDB file 1HTB

Broader image of alcohol dehydrogenase showing the enzyme in its entirety, as well as both active sites on each respective monomer.





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