Enterococcus faecalis is an important pathogen that is associated with a range of infections. Beta-lac tam antibiotics are a broad class of antibiotics that are used for treatment of E. faecalis infections, but it has int rinsic and acquired resistance to some of them. Penicillin binding prot ein (PBP) 5 is one of the members of PBPs family th at plays as inhibitors of beta-lactam antibiotics. In this stud y, we used an in silico strategy and focused on PBP 5 in E. faecalis and explained its characterization with the help of bioinformatics tools. The results of primary struc ture prediction showed that PBP5 is a stable protein and belong to hydrolase protein family. The secondary structure w as predicted that random coil is predominantly present followed by extended strand and alpha helix. The three-dimen sional structure was modeled using Swiss model workspace a nd the structure was validated that gives valuable understanding for the improvement of helpful ration al strategies for experiments. Ramachandran plot an alysis showed that 98% and > 99.8% of all residues of PBP5 were found in favored and allowed regions, respect ively. Computer simulation studies, including molecular mo deling, having knowledge of PBP5 structure and comb ination of this information may affect the development of n ew ways of inhibiting PBP5 to can be designed impro ved drugs.
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