Our MD simulation approach, based on the existing KRAS structural data, provides the first publicly available putative binding modes for the two KRAS(G12C) inhibitors GDC-6036 and LY3537982. Our results also suggest the putative bioactive atropisomer of LY3537982, which has not been disclosed to date. Generally, the simulations demonstrate the stable binding of both inhibitors in SII-P of KRAS(G12C). Our biochemical assays confirm the high potency of these compounds towards KRAS(G12C), and their effect on the double mutants (G12C/H95L, G12C/Y96D), these results both being in line with the observations of the simulations.