Antibiotic resistance is a major clinical issue which is going to cost millions of lives around the world by the year of 2050. The World Health Organization has disclosed the list of nosocomial bacterial pathogens that are gaining antibiotic resistance among which Pseudomonas aeruginosa is a prominent one. This culprit is a potential biofilm former, thereby resisting multiple antibiotics as well as our immune cells. Biofilms are complex aggregates of bacterial cells encased within extracellular polymeric substances. Biofilms are mainly composed of – Exopolysaccharides (40-95%), eDNA (1-10%), proteins (1-60%) and lipids (1-40%). Pseudomonas spp. can produce at least three extracellular polysaccharides to aid in biofilm production and they are Alginate, Pel and Psl. Bacteriophages, viruses that can infect and kill bacterial cells, can efficiently break the biofilm to get access to their host bacterial cells and infect them. Bacteriophages employ a particular type of enzymes called Polysaccharide Depolymerases to degrade the biofilm exopolysaccharides. In this research work, three Bacteriophage encoded Polysaccharide Depolymerase enzymes (Depolymerase-1, Depolymerase-2, and Depoymerase-3) that can target P. aeruginosa biofilm exopolysaccharides have been identified and the structure and functions of those enzymes have been investigated. The molecular weights of Depolymerase-1, Depolymerase-2, and Depoymerase-3 are – 50 KDa, 70 KDa and 75 KDa respectively. Electron microscopically they all are spindle shaped proteins. All three depolymerases are β-sheet rich trimers having three distinct domains – N-terminal domain, Central domain, and C-terminal domain. The monomers of Depolymerase-1, Depolymerase-2, and Depoymerase-3 have 397, 692, and 747 amino acid residues respectively. The X-ray crystallographic structure of Depolymerase-1 has been solved and analyzed. Depolymerase 2 and Depolymerase 3 are currently under the crystallization trials and so, the Alpha Fold structural predictions have been presented here.