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[Preprint]. 2023 Oct 16:2023.08.31.555822. Originally published 2023 Sep 1. [Version 2] doi: 10.1101/2023.08.31.555822

Figure 2. Hydrophobic interface anchors the Catalytic machinery to the αE-helix and αF-helix.

Figure 2.

(A). I150 (in red) from αE-helix plays an important role by docking to αF-helix and Catalytic loop. Three residues from β7, L172, L173, and I174 (in dark tan) assemble the hydrophobic surface from αE-helix to ATP pocket. L173 and I174 are part of C-Spine. R-spine are also shown in red. D220 bridges H158 from αE-helix to YRD motif. (B). The logo of spines shows how important those hydrophobic residues are. The sequence of β6-β9 segment is also shown.