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. 2022 Dec 22;13:980217. doi: 10.3389/fmicb.2022.980217

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Copyright © 2022 Zhang, Dong, Sun, Hu, Wang, Nie, Li, Wang, Pang, Pang, Lu, Yao and You.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The interactions and per-residue free energy decomposition between DPD or ML364 with DPD/AI-2 receptors. (A) The interactions between DPD or ML364 with LuxP protein of V. Campbellii. (B) The per-residue energy decomposition between LuxP with DPD or ML364. (C) The interactions between DPD or ML364 with PctA protein of Pseudomonas aeruginosa. (D) The per-residue energy decomposition between PctA with DPD or ML364. (E) The interactions between DPD or ML364 with TlpQ protein of P. aeruginosa. (F) The per-residue energy decomposition between TlpQ with DPD or ML364. Protein-ligand interactions are colored as following: blue solid line, hydrogen bond; dash line, hydrophobic interaction; cyan solid line, halogen bond.