Fig. 3

a Structural formulas show that the mutant amino acid residue is bigger than the wild-type amino acid residue (b) 3D structure of wild-type of Human SMS protein in ribbon presentation. Helices (shown in cyan color), Sheets (shown in magenta color) and loops (shown in orange color). c Overview of the protein in ribbon-presentation. The protein is colored grey, the side chain of the mutated residue is colored magenta and shown as small balls. d Zoomed 3D structure of wild-type of human SMS in ribbon presentation Helices (shown in cyan color), Sheets (shown in magenta color) and loops (shown in orange color). Serine is present at position 302 shown in green color. e Zoomed 3D structure of mutant SMS of human in ribbon presentation Helices (shown in cyan color), Sheets (shown in magenta color) and loops (shown in orange color). Serine is replaced by Leucine at position 302 shown in red color (f) Sequence alignment of SMS gene among different species. In the human sequence, amino acids from 301 to 360 are shown. The mutation site considered in this study was showing complete conservation among different species. Multiple sequence alignment is performed with Clustal Omega protein alignment tool