In the context of a polypeptide chain, the term "secondary structure" refers to the standard and recurrent spatial configurations of neighboring amino acid residues. Hydrogen bonds between amide hydrogens as well as carbonyl oxygens of the peptide backbone are responsible for its stability. Alpha-helices (α-helices) and beta-structures (β-structures) are the two most important types of secondary structures . The SOPMA program demonstrated that the protein contains alpha helix (239, 43.77%), extended strand (112, 0.51%), beta turn (23, 4.21%), and random coil (172, 31.50%). No Pi helix, beta bridge, bend region, and ambiguous states were present in the protein (Figure ). The selected protein contains polar, non-polar, aromatic groupcontaining, and hydrophobic amino acid residues in its structure (Figure ). Moreover, the sequence plot demonstrated the protein parameters, including the protein's helical, coil, and extracellular properties (Figure ). The secondary structure of the selected protein is illustrated in Figure .