Fig. 8

DynaMut tool depiction of molecular flexibility analysis and interatomic interactions of kinase domain of PKC γ. a Variant G360S is shown. Hydrogen bonds are present at 2.9A and 3.5 A distance. The region where mutation is present is highlighted with blue region inside the red highlighted box that depicts the rigidification of the structure. b Variant L403P is shown. Hydrogen bonds are present at 2.7A and 2.9A. The hydrophobic interactions are observed at 3.6A-4.5A. c Variant L468P is shown. Hydrogen bonds are present between 2.9A and 3.7A while hydrophobic interactions are observed at 3.9A-4.5A. d. Variant D480Y is shown. Hydrogen bonds are present between 2.9A and 3.3 and hydrophobic interactions are represented at 2.3A-3.9A. e. Variant Y521C is shown. Hydrogen bonds are present between 2.6A and 3.6A while the hydrophobic interactions are observed at 3.4–4.4A. f. Variant R597H is shown. Hydrogen bonds are present between 2.6A and 3.4A. Ionic interactions are displayed between 3.3A and 3.6A. The hydrophobic interactions are observed at 4.1A.The region where mutation is present is highlighted within red box that depicts the increase or decrease of molecular flexibility