D954 Nucleic Acids Research, 2012, Vol. 40, Database issue Figure 6. Use case for imatinib. The main panel (A) shows the compound synopsis for imatinib. The structure is shown with the murko scaffold highlighted in red. The banner at the top highlights certain properties indicated by icons which are active/inactive. From the left, the icons are active if the following properties are positive: is chiral, is rule-of ﬁve compliant, is solved in complex in a 3D structure, contains a toxicophore, is a clinical candidate, is a marketed drug, has a black-box warning, is oral, is injected, is topical and is a prodrug. Panel (B) displays the 3D structures solved in complex with Imatinib. Panel (C) shows the superposition of a SYK structure with an ABL1 structure. In green is the well-known DFG-out binding mode. In yellow is the alternative mode adopted in SYK when imatinib changes conformation and binds in a canonical, directly ATP competitive mode. search. Understanding likely binding modes for a compound, and whether there is evidence for them, is an important part of understanding mechanisms of com- pound effects and is very valuable in lead optimization. In this example, the drug imatinib is identiﬁed through a chemical search. Imatinib is known to bind to ABL1, but has subsequently been found to bind to a wider range of kinases. Bioactivities of imatinib against molecular targets or cell lines, together with any ADMET (Absorption, Distribution, Metabolism, Excretion and Toxicity) data available are summarized in the Compound Synopsis (Figure 6A). This page also allows obtaining these bio- activity data for a compound’s (in this case, imatinib) ana- logues. If a compound has been solved in complex in one or more 3D structures, a link from this page leads to the list of all 3D structures containing this compound. This allows identiﬁcation of valuable 3D data for the com- pound in any system in which it has been characterized, regardless of protein family or organism, as shown here for imatinib. Furthermore, the effective integration of structure comparison and ligand interaction maps allows comparison of binding modes for the compound. In this case, the structure of imatinib has been solved in complex with a wide variety of protein kinases (Figure 6B). Selecting any set of structures allows viewing structural superposition. Here, the structure of imatinib in complex with ABL1 and with Spleen Tyrosine Kinase (SYK) (42) are compared (Figure 6C). The superposition shows the alternative binding modes that imatinib adopts within the two kinases. Users can access a graph showing the RMS over the whole sequence and interact with this graph to highlight the areas of the superposition that have the most mobility. Additional example batch mode use cases are described in the Supplementary Data. CONCLUSIONS Here, we have presented the canSAR database and web interface for the integration of heterogeneous data for