Fig. 4: Conformational flexibility of mTOR on the membrane.

a, The intermediate and fully active states of mTOR are superimposed by overlaying their bound RHEB molecules. Movement between intermediate and active states is indicated with arrows. b, Close-up view of the interaction between residues 1,255 and 1,260 of mTOR and switch I of RHEB in the intermediate and active states. The cryo-EM density corresponding to switch I is shown (contour levels of 0.139 and 0.137 for the intermediate state and the fully active state, respectively). c, Close-up view of interactions between the FAT and C-lobe domains of mTOR, with insets indicating residues in the intermediate and fully active states. The FAT (residues 1,255–1,453 are omitted) and kinase domains of the intermediate and active states are superimposed on the basis of the C-lobe (residues 2,200–2,400). d, Different states of mTOR structures are superimposed on the basis of the C-lobe (residues 2,200–2,400). The distance of the γ-phosphate of ATP between soluble mTORC1–RHEB and the fully active state is shown in red.