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 dehydrogenase is an NADPH-dependent monomeric enzyme, which catalyzes the conversion of dehydroshikimate to shikimate, the fourth step in the shikimate pathway. This structure reveals that the N-terminal domain dehydroshikimate-binding domain has an alternating β-strand/α-helix character, whereas the C-terminal NADPH binding domain adopts a classical Rossman fold. In the asymmetric unit, four molecules forms two dimmers with the buried surface area of ~1800 A2. There is a single S-S bridge at the dimerization interface. The Rossmann fold domain is not involved in oligomerization. Each of the four molecules of the shikimate dehydrogenase has non-covalently associated shikimate. Binding of the ligand did not lead to big structural changes in the protein. Pairwise structural alignment of the apo-form and the binary complex structures reveals ~1.0 A r.m.s.d in the positions of the Cα atoms.