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3D Structural Analyses of Bifunctional Protein MdtA for Target Site Identification



Author(s)

Muhammad Zeeshan Ahmad

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DOI:10.17265/2328-2150/2023.03.002

Bifunctional Protein MdtA catalyzes the dehydrogenation of methylene-H4MPT. MdtA also catalyzes the reversible dehydrogenation of methylene-H4F with 20-fold lower catalytic efficiency. Multiple structure prediction approaches including comparative modeling, threading, and ab initio were utilized to predict the 3D structure of the selected protein followed by the validation of the predicted structures through Errat, Procheck, and mol probity. The predicted 3D structure of MdtA revealed 9 alpha helixes sheets having 98.92% overall quality factor. Interestingly, it was observed that only 1.1% residues were present in the outlier region while 97.9% in favored and allowed region with -8.96 prosA z-score value. The selected protein participates in glyoxylate and dicarboxylate metabolism. In conclusion, the structural insight analyses of MdtA may improve the reversible dehydrogenation of methylene-H4F leads to comparative molecular docking analyses.

3D structural insights, MdtA, in silico, Homology modeling, Bioinformatics.

Ahmad, M. S. 2023. "3D Structural Analyses of Bifunctional Protein MdtA for Target Site Identification." Journal of Pharmacy and Pharmacology 11 (3): 56-59.