Molecular recognition of carbohydrates by proteins plays a key role in many biological processes including immune response, pathogen entry into a cell, cell-cell adhesion and so forth. The list of proteins that recognise carbohydrates via aromatic residues include lectins, carbohydrate-binding modules, glycosidases, glycosyl transferases, “greasy slides” of carbohydrate transporters and complimentary sugar-binding sites (“sugar tongs”). Carbohydrates typically interact with aromatic systems in a parallel orientation. In this study we present the first systematic computational three-dimensional scan of carbohydrate hydrophobic patches for the ability to interact via CH/pi dispersion interactions. The carbohydrates b-D-glucopyranose, b-D-mannopyranose and a-L-fucopyranose were studied in a complex with a benzene molecule, which served as a model of the CH/pi interaction in carbohydrate/protein complexes.