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. 2020 Apr 14;10:6324. doi: 10.1038/s41598-020-63016-5

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© The Author(s) 2020

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Computational model of IPK1 with its substrate, its interacting proteins and identification of key mutations for catalysis inhibition. (A) Residue of IPK1 that interact with substrate IP₅. (B) Protein-protein interactions of IPK1 indicating associated proteins, revealed by databases and textmining. (C) Mutations that destabilize protein at 205 position and have the potential to hinder catalytic activity.