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. 2021 Jul 22;14:161. doi: 10.1186/s13068-021-02003-y

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 6 — Sugar substrates bound to ODH active site. a Top view (perpendicular to the isoalloxazine plane) and b side view of ODH-G3G: the protein is shown in green, the FAD cofactor in yellow, G3G in pink (β anomer) or magenta (α anomer). c Top view and d side view of ODH-GLC: the protein is shown in light blue, the FAD cofactor in yellow, GLC in orange (β anomer) or gold (α anomer); O atoms are in red, N atoms in blue. In both structures the β anomer is closer to the FAD cofactor than the α anomer, and oriented with hydrogen bonds between the reactive O1 atom and His528 and the FAD N5 atom. Both sugars are sandwiched on top of Tyr64 by the aromatic residues Phe421, Phe416 and Trp430. Water molecules are depicted as red spheres. Hydrogen bonds (distance < 3.2 Å) are represented with dotted lines