Figure 7
Conformational flexibility of binding site residues within studied structures. (A) Top left and right figures show the conformational flips of amino acids resulting in the absence of S1 subsite in 7DPU and 7DDC structures, respectively (blue—7RFS, green—7DPU, brown—7DDC). Bottom is the distributions of distances between Glu166 CD—Cys145 CA and Leu141 CG—Met165 CA, expressed in angstroms (Å) among studied crystallographic structures (B) Violin plot of the Probability Density Function (PDF) distributions of shortest distances between active ligands and the alpha carbon of Ser139 across all crystallographic and docked structures, expressed in angstroms (Å). (C) Trans and gauche conformations of the Met49 amino acids and corresponding closed (7RFS) and open (5RHE) states. (D) Violin plot of the PDF distributions of shortest distances between active ligands and the alpha carbon of Thr25 across all crystallographic and docked structures, expressed in angstroms (Å).
