BACKGROUND: Shiga Toxin-Producing Escherichia coli ( OBJECTIVE: This study aims to evaluate Glutamate Racemase (MurI protein) of the food-pathogenic METHODS: Using computational tools, the study identified inhibitor binding sites on EC MurI and identified relevant inhibitors capable of binding to these sites. Molecular docking techniques were employed to assess potential hits, and selected compounds were further analyzed for their structural activity and binding affinity to the protein. RESULTS: The results of the study revealed that Frigocyclinone and Deslanoside, exhibited the best binding affinity with EC-MurI. Subsequent molecular dynamic (MD) simulations of the selected complexes indicated that both compounds were stable. This suggests that Frigocyclinone and Deslanoside have the potential to serve as potent inhibitors of EC-MurI. CONCLUSION: In summary, this study highlights the urgent need for alternative therapies against food-pathogenic