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. 2019 Jan 28;24(3):465. doi: 10.3390/molecules24030465

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The results of the molecular docking (MD) simulation of the SrtA-astilbin complex. (A) The root-mean-square deviations (RMSD) exposed by the backbone atoms of the protein during the MD simulation of the SrtA-astilbin complex. (B) Decomposition of the binding free energy on a per residue basis in the SrtA-astilbin complex. (C) The predicted interaction mode of astilbin with the amino acid residues of the catalytic center of SrtA. (D) The inhibition effect of astilbin (64 μg/mL) (A represents astilbin) on the activities of SrtA and its mutants L111A-SrtA, L116A-SrtA, and R213A-SrtA. Significant differences between groups were accepted at * p < 0.05 and **** p < 0.0001.