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.