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. 2021 Jan 4;4:28. doi: 10.1038/s42003-020-01531-x

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© The Author(s) 2021

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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Fig. 5 — a Electrostatic surface representation of AtCRY2-PHR_tetramer and close up of FAD (yellow) binding cavity. Electrostatic potential is color coded on the surface with red and blue representing areas of negative and positive charges, respectively. b Interactions of AtCRY2-PHR_tetramer with FAD. FAD in yellow is colored with carbon (black), nitrogen (blue) and oxygen (red). Dotted lines in black represent hydrogen bonds between AtCRY2-PHR_tetramer and FAD. Hydrophobic interactions are shown as spoked arcs (red) (prepared by LigPlot). c Close up view of FAD (yellow) and diverged residues within the binding pocket of AtCRY2-PHR_tetramer (D393, light blue) superposition with AtCRY1 (D396, green, PDB: 1U3C), Arabidopsis, AtCRY3 (N428, Magenta, PDB:2VTB), Agrobacterium tumefaciens Photolyase, AgPL (N380, blue, PDB:4U63)⁴¹, Escherichia coli Photolyase, EcPL (N378, Yellow, PDB: 1DNP)⁶⁴, and Anacystis nidulans Photolyase AnPL (N386, orange, PDB:1TEZ)⁶⁵. d Comparative analysis of plant cryptochromes tryptophan triad positions in relation to FAD. Residues are colored as in c. Distances were measured with PyMOL and indicated in dotted lines.