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. 2019 Feb 4;9:1132. doi: 10.1038/s41598-018-36213-6

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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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Molecular modeling studies defining the property of the binding site. (A) Electrostatic surface potential map of CSN-MN representing the very acidic binding site; red, acidic regions; blue, basic regions. (B) The 4C1 chair conformation was observed as the major conformation during simulation, changes in the dihedral angles at the different time points of simulation at subsite (−1) indicate switches in the pyranose ring conformation (see also Fig. S5). (C) Enzyme-substrate interaction map between CSN-MN and GlcN₆ as a substrate showed all possible interactions; catalytic residues E74 and E261 are highlighted in khaki color, aromatic residues making stacking interactions with the substrate are colored in green, and acidic residues are colored in violet. (D) The distance measured between the catalytic residues E74 and E261 during simulation (average 7.4 Å) indicates that CSN-MN is an inverting enzyme.