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    Journal of Pharmacology and PharmacotherapeuticsNOW IN
    Article

    In Silico Modeling and Docking Analysis of CTX-M-5, Cefotaxime-Hydrolyzing β-Lactamase from Human-Associated Salmonella Typhimurium

    S. K. Md. Jasmine1, Vidya Sagar Reddy G.1, Neelima Gorityala2, Someswar Rao Sagurthi2, Sandhya Mungapati3, Kota Neela Manikanta4, Uday Sankar Allam1★★ Corresponding author

    1. 1Department of Biotechnology, Vikrama Simhapuri University, Nellore, Andhra Pradesh, India.
    2. 2Department of Genetics and Biotechnology, Osmania University, Hyderabad, Telangana, India.
    3. 3Department of Crop Production, DAATTC Center, Acharya N G Ranga Agricultural University, Nellore, Andhra Pradesh, India.
    4. 4Department of Travel and Tourism, Vikrama Simhapuri University, Nellore, Andhra Pradesh, India.

    CORRESPONDENCE

    Uday Sankar Allam

    Department of Biotechnology, Vikrama Simhapuri University, Nellore, Andhra Pradesh 524324, India.

    vsuusareddy@gmail.com

    Received: 14-01-2022; Revised: 28-05-2022; Accepted: 09-07-2022.

    Volume 13, Issue 2 · pp. 135–147 · PUBLISHED 2022 · DOI: 10.1177/0976500X221109721

    View on J Pharmacol. Pharmacother. original site ↗

    ABSTRACT

    Objective: To computationally model the CTX-M-5 β-lactamase and establish its structure, which is exclusively present in human-associated Salmonella. Methods: The CTX-M-5 aminoacid sequence (Uniprot ID:O65975) of Salmonella enterica subsp. enterica serovar typhimurium was retrieved from UniProt database and subjected to homology modeling using MODELLER 9v7. The homology models were duly validated using RAMPAGE tool by generating Ramachandran plots, ERRAT graphs, and ProSA score. DoGSiteScorer server and ConSurf server were used to detect the cavities, pockets, and clefts to identify conserved amino acid sites in the predicted model. Subsequently, the modeled structure was docked using CLC Drug Discovery Workbench against proven drugs and known inhibitors. Results: Obtained high-quality homology model with 91.7% of the residues in favorable regions in Ramachandran plot and qualified in other quality parameters. Docking studies resulted in a higher dock score for PNK (D-benzylpenicilloic acid) molecule when compared to other reported inhibitors. Conclusion: This in silico study suggests that the compound PNK could be an efficient ligand for CTX-M-5 β-lactamase and serve as a potent inhibitor of CTX-M-5.

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      Jasmine, S. K. M., G., V. S. R., Gorityala, N., Sagurthi, S. R., Mungapati, S., Manikanta, K. N., & Allam, U. S. (2022). In Silico Modeling and Docking Analysis of CTX-M-5, Cefotaxime-Hydrolyzing β-Lactamase from Human-Associated Salmonella Typhimurium. Journal of Pharmacology and Pharmacotherapeutics, 13(2), 135–147. https://doi.org/10.1177/0976500X221109721