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. 2024 Feb 27;29(5):1024. doi: 10.3390/molecules29051024

Figure 4.

Figure 4

(a) Superimposition on the backbone atoms of EphA2–Sam NMR structure (first conformer, pdb entry 2E8N after removal of the flexible N- and C-terminal tails, residue range T908 to V972) (light grey) and the EphA2–Sam wild-type AF2 [24,58] model (violet). The backbone of residue Ile 944 is highlighted in black. (b,c) Overlays on the backbone atoms (residue range T908 to V972) of AF2 models of EphA2–Sam wild-type (violet) and cancer related mutants (dark green): (b) R950W, (c) R957C. The backbone of mutated residues is coloured yellow on the ribbon representations. The side chains of native and mutated residues are shown in violet and yellow, respectively in the upper left inserts (b,c). The EH surface in all panels is coloured in red (residues I916–M918 and P952–Y960), RMSD values are also indicated in each panel.