To explore the range of applicability of the PhABit platform, we subsequently applied it to KRas, which has been widely reported as a protein with low tractability towards small molecule binders. KRas oncogenic driver mutations are found in 30% of cancers. The mutations result in constitutive activation of KRas and downstream signalling pathways which promote uncontrolled cell proliferation and survival. The inhibition of KRas has been widely investigated for the development of oncology therapeutics, however, due to the lack of well-defined binding pockets on the protein it has proved extremely challenging to develop potent ligands. Some success has been reported using fragment screening, which enabled identification of micromolar, and recently submicromolar, ligands to a shallow pocket between the switch I/II regions of KRas. KRas fragment screening has typically employed HSQC NMR with 15 N-labelled protein, which is resource intensive. We explored whether the PhABit library could provide an alternative approach to identify fragment binders and their binding sites.