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. Author manuscript; available in PMC: 2015 Jul 3.
Published in final edited form as: Mol Biosyst. 2014 Apr 29;10(7):1890–1904. doi: 10.1039/c3mb70620f

Figure 5.

Figure 5

Results for docking the peptide Y1173 to EGFR TKD. A) Six predicted peptide clusters of the Y1173 bound conformations generated by ensemble docking that satisfied the distance criteria in panel A. The bi-substrate peptide binding pocket is shown in the background, for reference. All 6 conformations were re-ranked using the MMPBSA method (see Table 2). B) A depiction of the main interactions between the peptide and kinase: Y(P0) hydrogen-bonds with D813; E(P−1) forms a salt bridge interaction with residue K855; hydrophobic residue L(P+1) interacts with a hydrophobic surface in EGFR TKD consisting of residues V852-P853-I854-W856. All hydrophobic residues are depicted as transparent surfaces.