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. 2017 Jun 6;7:2876. doi: 10.1038/s41598-017-03003-5

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© The Author(s) 2017

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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Surface representation of the garlic mannose-binding lectin protein (monomer, chain A). The residues are colored by closeness values with red, orange and cyan corresponding to the high (top 20%), intermediate (20~60%) and low (below than 60%) closeness values. The crystal structure of garlic lectin showed that THR5 is responsible for dimer formation and snowdrop lectin indicated that ASP17/GLU19 might be responsible for tetramer formation.