The three-dimensional form of a protein is known as its tertiary structure. One primary 'backbone' polypeptide chain in the tertiary structure comprises one or more protein secondary structures (PSSs) called domains . There are a variety of possible interactions and bonds between amino acid side chains. The sequence-structure gap (SSG) is a significant obstacle in computational biology and chemistry, and protein structure anticipation is one strategy to close this gap. Accurately predicting the structure of a protein is critical since protein structure dictates its function . The most favored protein templated (HHpred ID: 2B9B_A) was selected for anticipation of the three-dimensional protein structure by the Modeller program with the HHpred interface with the probability of 100%, E-value 2.8 × 10 -132 , and target length of 497 (Figure ).