Abstract: Molecular docking is an efficient computational tool to predict the structures of protein-ligand complex. This kind of simulation is of fundamental importance for interpretation of numerous biochemical phenomena, providing useful information on the preferred binding sites of ligands, and therefore in rational drug design. Bovine β-lactoglobulin (BLG) is a small extracellular protein belonging to the lipocalin superfamily. Lipocalins have been classified as transport proteins with the remarkable ability of binding small hydrophobic molecules within the central cavity also known as calyx. Because of its stability, abundance and easiness of preparation BLG, has been frequently studied to clarify its structural and binding features. Several studies suggest that more than one binding site exists, thus the aim of this work is to investigate the existence of other sites, in addition to the calyx one, and to verify if BLG can interact and play the role of carrier of drugs. We considered the particular case of Norfloxacin which is a broad-spectrum antibiotic used in treatment of urinary tract infections.