Skip to main content
. Author manuscript; available in PMC: 2008 Sep 17.
Published in final edited form as: J Med Chem. 2007 Aug 3;50(17):3980–3983. doi: 10.1021/jm070645a

Figure 3.

Figure 3

(A) Sequence alignment of YpkA (115-431) with protein kinases P38 and ERK. Strict sequence conservation is shown in red background, and strong sequence conservation in yellow. The solvent-accessibility of each residue in the P38 structure is indicated in the bar at the base of the sequences, with white representing buried residues, dark blue representing solvent-accessible residues, and light blue representing an intermediate value. The secondary structural elements are also indicated according to the structure of P38. (B) Structural alignment of the two homology models of YpkA kinase domain. Model A (red) represents a conformation of YpkA with an open ATP-binding pocket, while model B (cyan) has a closed ATP-binding pocket. The key residues to the ligand binding are shown in magenta.