Fig. 7.

Interatomic interaction analysis of wild-type and mutant PDE6 catalytic residues a) depicts Asp-600 (cyan colored) bound to cGMP (white), Mg²⁺ (green sphere) and nearby residues (green) within the catalytic pocket. Ionic interactions (blue), hydrogen bonds and van der Waals (red color), hydrophobic interaction (grey small dotted lines) and carbon-π interactions (dark grey dotted lines). b) Illustrates interaction network of missense mutation Asn-600 (labelled in red) with cGMP (white), Mg²⁺ (green sphere) and surrounding catalytic residues (green). Hydrogen bonds are shown in red dotted lines whereas donor-π interaction with wheat colored dotted lines. c) Shows dense network of hydrophobic and ring interactions between Phe-742 (cyan), cGMP (white) and surrounding catalytic pocket's residues (green). Hydrogen bonds are depicted in red dotted lines, atom-ring interactions including methionine -π interactions and carbon-π interactions are shown in dark grey dotted lines. Proximal hydrophobic interactions (small grey-dotted lines) and undefined interactions are shown as dense network of small dots. d) Illustrates dense proximal hydrophobic interaction network (small grey dotted lines) of missense mutation F742 L (Leu-742 labelled with red) with neighboring residues (green). Loss of interaction between cGMP (white) and Leu-742 is also depicted in graphical depiction. e) graphical illustration of Intermezzo analysis of F776 (cyan) with cGMP (white) and nearby surrounding residues (green) of catalytic domain of PDE6. Hydrogen bonds are shown in red dotted lines, hydrophobic interactions are shown in small dotted lines, ring-ring interactions between F776 and cGMP are shown in grey dotted lines while carbon-π interactions of F776 with neighboring residues are shown in wheat color. f) Illustrating hydrogen bond (red dotted lines) and carbonyl interaction (magenta color) of missense mutation Leu-776 (F776 L labelled in red) with neighboring residues (green). Loss of binding between F776 L and cGMP was also observed in intermezzo analysis.