Plastic usage has increased dramatically in recent years in which polyethylene terephthalate (PET) is one of the most abundant types of plastic waste. Researchers had discovered a number of microorganisms that have plastics degrading enzymes, and Ideonella sakaiensis is one of the most studied examples of an organism that has a PET-degrading enzyme. These well-known enzymes degrade PET at a moderate turnover rate, though. Therefore, more study is required to improve the variety of microbes and enzymes that can break down plastic. In this study, molecular docking analysis was used to find the IsPETase homologue enzymes that can bind to the PET ligand. Their capacity to bind to PET indicates that it might be a potential enzyme that breaks down PET. The molecular docking predicted a novel alpha/beta hydrolase (7CUV and 7E31) as the most potential candidate enzyme for PET-degrading activity (ΔG value: -6.8 kcal/mol and -5.2 kcal/mol, respectively). With ΔG values of -5.5 kcal/mol and -5.7 kcal/mol, respectively, an esterase with a long N-terminal extension (LNTE) isolated from a leaf-branch compost (3WYD) and a lipase referred to as SeL from Streptomyces exfoliatus (1JFR) also demonstrated a promising binding affinity to PET. In conclusion, computational techniques such as in silico molecular docking analysis, in conjunction with the expanding databases of enzyme and genomic information, offer the potential to quickly uncover new enzymes and microorganisms with the capacity to breakdown PET. To further confirm these possible enzymes, lab-based methods such as biochemical, structural, and others are required.