Penicillin binding proteins have been a well established target for antimicrobial therapy. β-lactum antibiotics the widely used inhibitor for PBPs inhibits the transpeptidase activity of PBPs by forming a covalent penicilloyl-enzyme complex which blocks the normal transpeptidation reaction; resulting in bacterial death. Resistant bacteria tend to distort the active site of PBP thereby lowering their acylation efficiency for β-lactams. We have tried to find a solution for this problem with the use of noncovalent inhibitors of PBPs. In order to explore the possibilities of a new drug, 3, 5, 6-trichloro-2-pyridinol (TCP) the hydrolysis product of Chlorpyrifos a broad spectrum moderately toxic organophosphorus insecticide was chosen in this present study. This is the first study which focuses on the use of TCP as a likely drug candidate against commonly encountered pathogens. Four Gram negative bacterial pathogens Escherichia coli (3MZD and 1NZO), Pseudomonas aeruginosa, Shigella dysenteriae and Klebsiella pneumoniae and two Gram positive bacterial pathogens Staphylococcus aureus and Streptococcus pneumoniae were selected for this study and were identified using standard biochemical tests. TCP had a good inhibitory effect against these pathogens, it was found to be most effective against Pseudomonas aeruginosa and Staphylococcus aureus with a zone of inhibition of 22mm and 21mm respectively. TCP was equally effective against Salmonella typhimurium, Shigella dysenteriae, Klebsiella pneumoniae and Escherichia coli -3MZD (20mm each). Insilico analysis was also performed by choosing Penicillin Binding Proteins of the microbes as the target protein sequence. iGEMDOCK is the docking tool used for docking TCP against all of these PBPs. Pseudomonas aeruginosa registered the best docking score of -66.5(which correlates with 22mm zone of inhibition) followed by the others.