Protein kinases are a well-established class of clinically useful drugs, particularly for the treatment of cancer. The protein kinase family, the Kinome, that binds ATP present a very similar alignment of binding site residues and hence it is often challenging to design selective inhibitors. However, achieving selectivity can be critically important in drug design pipelines to avoid off-target effects. In this report we highlight how the FP-score classification of binding site residues using static FMOPhore mode in scanning the apostructure of two protein kinase systems, Protein Kinase B (PKB) and Janus Kinase-2, JAK-2. can be used to drive selective design.