 Associated Research Director of Origin Discovery Technologies, a software storey company based in Bangalore, India. These are my products, under the service of Mr. Arasimhan, who is the Director of Origin Sciences Department, and Arasimha Rao, who is the Christopher Field Department. This work described in this 14 cents article was carried out as part of a collaboration with the University of Mariah to develop antibacterial compounds to treat mediviruses. This is an infectious disease caused by the gram-active organism orchid-area pseudomaline that affects both humans and animals. This infection is recognized as an important health problem in southern stations, countries, and tropical north demonstration. Clinical manifestations of mediviruses include pneumonia with or without septicemia or localized infections involving the skin and the soft tissue organs. Current treatment options include self-tracidine or carbapenemosibutrosine for two weeks during the initial intensive phase of therapy, followed by 12 weeks of oral therapy. Apart from the long duration, another issue with this treatment is the reported drug resistance, which is the hallmark of bacterial infections. So, there is an urgent need for developing new drugs that function through novel mechanism of action, which is a challenging task. The parietic acid via synthesis pathway is a relatively unexplored area for antibacterial drug development. This pathway is unique in bacteria as compared to that in humans. In bacteria, individual enzymes catalyze each stage of parietic acid via synthesis, whereas a single multi-enzyme formulas mediate parietic acid synthesis in humans. Therefore, it is possible to selectively inhibit parietic acid via synthesis in bacteria without affecting that in humans. There are several enzymes in this pathway. Enoïdic pyrlectase, also known as papi, that catalyzes the final step in each cycle of bacterial parietic acid synthesis, utilizing NADH or NADPH as a papi drug, is known to be a critical enzyme for the survival of bacteria. Therefore, we initiated a project to develop inhibitors for papi, for drug development, and then work order is humanized in functions. So, several compounds inhibiting papi from different organisms have been identified, among which AFN1252 is one of the most advanced inhibitors in phase two clinical development, which is selected for gram-positive bacteria. In an effort to identify inhibitors of bercoultary of fabi, we screened several compounds using a biochemical assay, which was established with an inhose purified protein. To our surprise, we found AFN1252 to be a very potent inhibitor of BPM fabi, with an IC50 of around 9 nanomolar, and also this inhibitor showed antibacterial activity against bercoultary of pseudomalli R15 strain, which was isolated from patients with melidiosis. In order to understand the binding mode and the mechanism of action of binding, we conducted thermal melting temperature studies, kinetic studies, and also, it states To begin with, with thermal melting studies, we found that the AFN1252 compound stabilizes bercoultary of protein in the absence of cofactors NADH or NADPH. This binary mechanism of binding is different in contrast to the terminal mechanism reported elsewhere for fabi inhibitors in the presence of cofactor and the protein. Data from kinetic studies carried out by varying the substrate, protonal 4a and cofactor NADH at different concentrations of AFN1252 suggested a mixed mode of inhibition were able to obtain diffraction quality crystals. However, when we saw the structure, we observed that the density corresponding to NADH was not seen. To further explore the mechanism of binding, we saw the crystal structure of AFN1252 complex at a resolution of 2.3 angstrom and the data presented here gave clear evidence that a binary complex formation between AFN1252 and AFN1252 is possible. This is in contrast with all the earlier reported crystal structures of AFN1252, b with equal i, climaidia or staphylococcus, wherein the inhibitor binds to the enzyme in presence of the cofactor NADH. Fibium fabi AFN1252 complex for a symmetrical datametric structure with one molecule of AFN1252 go to each monomer of the BPM fabi. Hydrogen bonding, hydrophobic contacts and water-mediated interactions stabilize the binary complex formation. Thus the data presented in this article clearly indicates a novel mechanism of action for AFN1252 binding to BPM fabi. The structural and mechanistic insights from these studies might help in rational design and development of new fabi inhibitors to treat malaria disease. Thank you.