The growing use of plastics like polyethylene terephthalate (PET) has led to increased pollution and a need for sustainable ways to break down these materials. One promising approach is using microbial enzymes through biocatalysis. This study focuses on a hydrolase enzyme from Thermobifida Fusca (T. Fusca), a heat-loving bacterium known for its stable and active properties at high temperatures, making it ideal for industrial use. The main aim of this research is to predict the 3D structure of this hydrolase using homology modelling and other computational methods. The predicted structure was carefully validated using structural assessment techniques such as the Ramachandran plot to ensure high accuracy and reliability. Sequence alignment analysis helped identify evolutionary traits and potential catalytic sites, offering insights into how the enzyme functions and interacts with PET and other substrates.