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. Shikimate kinase catalyzes the fourth step in the pathway. The structure reveals distinct sites for ATP and shikimate. Interestingly, within the asymmetric unit's three molecules two conformational states of the ATP binding site and three states of the shikimate binding site are observed.