Specific interaction study of complex between S-014-1049 and SK
using bioinformatics tool
S-014-1049 was found to be non-toxic to the vero cells. Complex study of
S-014-1049 with SK was done to check the specific binding of this
compound to different domains of the enzyme. The binding result showed
residues GLY14, LYS15, SER16, THR17, and ARG117 in binding region of the
compound. LYS15 forms hydrogen bond with fluorine atom (F3-N) of the
ligand at 3.2Å. Similarly, nearby residues such as GLY14, THR17 and
SER16 also make hydrogen bond with fluorine atoms (F1, F2 and F3).
ARG117 also forms hydrogen bond with fluorine atom. ASP34 form pi-anion
interaction with 3.84Å distance which is an unfavourable interaction.
The other residues which come in binding region are PRO118, LEU119 and
PHE49, these residues form hydrophobic interaction with ligand at
>4Å distance. From the study we can conclude that this
compound interacts via strong hydrogen bond with several residues of CD
as well as with one residue (ARG117) of LD (Figure 1C).