Protein structure and function is inextricably linked. Helix, coil, sheet, and turn are secondary structural elements that have a fantastic association with protein function, structure, and engagement . The secondary-structural element of the protein (QBQ56721.1) was predicted by the SOPMA software when the alpha helix (Hh), extended strand (Ee), beta turn (Tt), and random coil (Cc) were 60 (17.05%), 87 (24.72%), 20 (5.68%), and 185 (52.56%), respectively (Table ). The PSIPRED software predicts the helix, strand, and coil of the matrix protein (QBQ56721.1) with more confidence (Figure ). Table shows the amino acid composition obtained from the ExPASy service's ProtParam Tool. and 0.7 percent of residues were in the generously allowed regions [a,b,l,p]. The total number of non-glycine and non-proline residues was 301; the end-residues (excluding Gly and Pro) were 1; the glycine and proline residues were 27 and 13, respectively, out of 473 total residues (Table ). Verify 3D; a tertiary structure evaluation tool was used to demonstrate that the anticipated tertiary structure passed the evaluation.