To overcome this problem, we performed a post-docking analysis using structural proteinligand interaction fingerprints (SPLIF). SPLIF analysis allows for the quantitative evaluation of whether a compound's docking pose interacts with the protein target in a manner similar to any known ligand, and it can identify real poses that may have been penalized by a poor initial docking score. Indeed, using a test set of five randomly selected protein-ligand structures from the PDB, we found that the combination of the induced fit docking and SPLIF similarity scores allowed us to select considerably more accurate poses of the test ligands within the colchicine site of tubulin, compared to the docking score alone (Fig. ). Encouraged by this result, we applied the induced fit docking, enhanced by the SPLIF analysis, to predict the likely binding poses of compounds 2a and 3a (Fig. ).