Fig. 4: Solvent exposure of the inhibitors and the binding site residues.
From: Decisive role of water and protein dynamics in residence time of p38α MAP kinase inhibitors
a Solvent accessible surface area (SASA) of 1 and 2. b Solvent accessible polar surface area of 1 and 2. c Buried surface area (non-solvent exposed) of 1 and 2. d Buried polar surface area of 1 and 2. The black horizontal line in the box represents the median. Box displays the quartiles of the dataset (25–75%) and whiskers the rest of the data with maximum 1.5 IQR. Outliers are indicated with black diamonds. e Hydrophobic residues in the binding site that were monitored for their side chain solvent exposure are shown in stick model with their molecular surfaces illustrated in yellow. Compound 2 is shown in ball and stick model. Solvent exposure of Val38 (f), Leu74 (g), Leu75 (h), Leu171 (i), and Phe169 (j). f–j The blue background indicates solvent exposure (where ≥1 water molecule is located within 3 Å of the side chain) and the yellow background indicates when the side chain is not exposed to solvent. Solvent exposure of Val30, Tyr35, Ala51, Met78, Ile84, Leu104, Ala157, and Leu167 is shown in Supplementary Fig. 9. k Intra-protein salt bridge frequencies to catalytic Lys53. Simulation data was analysed for each 1 ns i.e., data in a–k consist of 91,328 and 86,505 individual data points for 1 and 2, respectively. Source data are provided as a Source Data file.
