Understanding molecular recognition during ligand binding is crucial for rational drug design. Protein kinases are a well known pharmacological target, especially in the therapeutic area of cancer. Solved crystal structures of tyrosine kinase domains in complex with ligands deliver insight into the binding event. These experimental data were collected and analysed by means of molecular modelling techniques. Common molecular recognition patterns were depicted and studied among this class of proteins. The results of this analysis and the consequences for rational design of inhibitors are presented.