Figure 3.

The molecular docking of wild and mutant with elastase‐2. Both the (upper figure) wild (D₆₁₄) and (lower figure) mutant (G₆₁₄) version of S protein was shown in golden color, whereas the elastase‐2 docked to D₆₁₄ and G₆₁₄ in blue and green color, respectively. The enlarged views of the docked site were shown in separate boxes. (A) The possible docked residues (stick model) on the wild S protein (warm pink) and elastase‐2 (green) are 618(Thr)−619(Glu)−620(Val) and 198(Cys)−199(Phe)−225:227 (Gly, Gly, Cys), respectively. The aspartic acid at 614 is 17.3°A far away from the valine (101), apparently the nearest aa of elastase‐2 to the cleavage site (615–616). (B) The possible interacting residues (stick model) on the mutant S protein (blue) and elastase‐2 (warm pink) are 614(Gly)−618(Thr)−619(Glu)−620(Val) and 101(Val)−103(Leu)−181(Arg)−222:227(Phe, Val, Arg, Gly, Gly, Cys), and 236 (Ala), respectively. In this case, the glycine at 614 is 5.4°Afar from the valine (101), the nearest aa of elastase‐2 to the cleavage site (615–616)