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. 2023 Sep 14;13:15234. doi: 10.1038/s41598-023-42504-4

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Docking poses LPA in FABP3, FABP5, and FABP7. LPA engages in numerous H-bonding interactions with (A) R126, Y128, and R78 in FABP3, (B) C45, T58, R111, C122, and Y133 in FABP5, and (c) I51, T53, T60, I62, and R106 in FABP7. (D–F) The orientation of LPA in (D) FABP3, (E) FABP5, and (F) FABP7. Note the solvent exposure in FABP5 and FABP7. The orientation of LPA also induces van der Waals clashes with (D) T73 in FABP3 and (F) I51, T53, T56, E61, and I62 in FABP7 to reduce binding affinity.