The role of water molecules and its dynamics to the binding site of β-lactamase enzyme with respect to β-lactamase inhibitor

β-lactamase hydrolyses amide bond of β-lactam ring. antibiotics are the main arsenal in antibiotic regime. High degree mutation and genetic variation enzymes have elevated resistance towards inhibitors. There 4 classes β-lactamase, namely Class A, C, D which Serine proteases B is Metallo proteases. The most documented one TEM, where water molecules (315, 319, 440, 441) play an important role binding site. In present work we tried to explain involvement molecule with respect docking behavior S70 (Serine), E166 (Glutamate) N170 (Asparagine) along Ω – loop (R161-D179) allosterically modulate This will aid us identify potential candidates as novel precisely interacting substrate site their interaction these molecules. We docked Clavulanic acid (CA), Sulbactam (SB), Tazobactam (TB) wild (1ZG4) mutated (1ZG6) TEM presence absence HOH, justifies importance playing hydrolysis well modulating affinity a drug candidate.