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. 2019 Feb 6;9:1506. doi: 10.1038/s41598-018-37815-w

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© The Author(s) 2019

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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Homology modeling of the GmSHMT08c. (A) One SHMT subunit with highlighted catalytic sites, PLP and THF cofactor binding and oligomeric structural residues labelled. (B) Dimer with highlighted residues. (C) GmSHMT08c gene model showing the residues conserved for catalysis, PLP and THF cofactor binding, and oligomeric structure maintenance. (D) Polymorphisms presented by all the thirteen GmSHMT gene family members at important conserved residues cited previously.