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. 2014 Dec 10;290(4):1936–1951. doi: 10.1074/jbc.M114.598698

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FIGURE 8. — Comparison of N⁶-(benzyl)-ADP (BZ-ADP) interactions in the nucleotide-binding pocket of AS and WT PKCδ. Shown are the superimposed structures of BZ-ADP (colored by atom type) and ATP (yellow) in AS (A) and WT PKCδ (B). Ala-427 is highlighted in purple in AS PKCδ, and Met-427 is highlighted in green in WT PKCδ. Shown are the BZ-ADP-interacting residues in the nucleotide-binding pocket of AS (C) and WT PKCδ (D). ATP interacts with the residues in the glycine-rich loop (red asterisks) and the invariant Lys-378 (red arrowheads). The gatekeeper is indicated by a red arrow.