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. 2022 Feb 11;5:126. doi: 10.1038/s42003-022-03085-6

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© The Author(s) 2022

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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Fig. 7 — a Structural alignment of PsKAI2A and PsKAI2B shown in pink and light green colors respectively. RMSD of aligned structures is shown. b Analysis of PsKAI2A and PsKAI2B pocket volume, area, and morphology is shown by solvent accessible surface presentation. Pocket size values were calculated via the CASTp server. c Residues involved in defining ligand-binding pocket are shown on each structure as sticks. Catalytic triad is shown in red. d Residues L/M160, S/L190, and M/L218 are highlighted as divergent legume KAI2 residues, conserved among all legume KAI2A or KAI2B sequences as shown in reduced Multiple Sequence Alignment from Supplementary Fig. 3.