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. 2016 Apr 16;16:87. doi: 10.1186/s12870-016-0773-9

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© Ghosh and Islam. 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 8 — Three dimensional homology model structure of soybean glyoxalase proteins. Structures of GmGLYI-3 (a), GmGLYI-16 (b) and GmGLYII-5 (c) were built using Swiss-model server based on available close similar structure from Protein Data Bank (PDB) Zea mays GLYI (5D7Z), mouse GLYI (4OPN), and AtGLYII-2 (2Q42) proteins, respectively. All the α-helices were marked with orange colour, while β-sheets were marked with cornflower blue. The active sites residues were identified based on the alignment with template structure and shown by ball-stick model. The structure and active residues were visualized and generated using chimera program