The shikimate pathway links metabolism of carbohydrates to biosynthesis of aromatic compounds. In a sequence of seven steps, phosphoenolpyruvate and erythrose 4-phosphate are converted to chorismate, a precursor of the aromatic amino acids and many secondary aromatic metabolites. The shikimate pathway is essential for most bacteria and plants but absent in humans, making it an attractive target for the development of novel antibiotics. Dehydroquinate synthase is a metalloprotein which catalyzes the nicotinamide adenine dinucleotide (NAD)-dependent conversion of 3-deoxy-7-phosphoheptulonate synthase to dehydroquinate, the second step in the shikimate pathway. This structure consists of an N-terminal NAD binding domain and an alpha-helical C-terminal domain. Clear electron corresponding to a bound NAD molecule is observed at the active site.