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. 2021 Aug 12;11:16427. doi: 10.1038/s41598-021-95941-4

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© The Author(s) 2021

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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Api5 interacts with p300 in silico. (a) Various acetyl transferases and their probability to acetylate lysine 251 of Api5 represented as p value using ASEB webserver, where lower p value corresponds to a higher probability. (b) The lowest-energy docking position of Api5 and p300 analysed using HADDOCK webserver and output analysed using PIZSA represented as a cartoon diagram. (c) Interaction between Lysine 251 of Api5 with p300. (d) Various amino acid interactions between Api5 and p300.