Fig. 6: X-Ray Crystal Structure of IDH1R132H complex with AG-120 (Ivosidenib).
From: Biostructural, biochemical and biophysical studies of mutant IDH1
a AG-120 sits between the IDH1R132H dimer interface, engaging in extensive hydrophobic interactions. b AG-120 forms a hydrogen bond with the side chain of Ser280 of chain A and is also within the hydrogen bond distance of the side chain of Ser277 (chain A). c The surface representation of AG-120 binding pocket. d The cyanide pyridine end of AG-120 is situated next to the side chain of Cys269 of chain B, leading to the possibility that AG-120 might covalently modify Cys269 through its nitrile moiety (shown in yellow). e Comparisons of AG-120:IDH1R132H and compound-1:IDH1R132H crystal structures.
