Structure of an IDH2 inhibitor (AGI-6780, structurally related to enasidenib and ivosidenib) allosterically bound at the homodimerization interface with detailed interaction diagrams to the right. Note the location of the Ile 319 and Gln 316 in the bottom right with critical hydrogen bonds to Gln 316. (Reprinted with permission from Chen J, Yang J, Sun X, et al. Allosteric inhibitor remotely modulates the conformation of the orthestric pockets in mutant IDH2/R140Q. Sci Rep. 2017 Nov 28;7:16458. http://creativecommons.org/licenses/by/4.0/)