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. 2019 Sep 23;9:13700. doi: 10.1038/s41598-019-50105-3

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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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Binding of ferricyanide in the active site of MvBOx wild type and its W396A mutant. (a) Binding of ferricyanide in OS1 of the WT:FECN structure (6I3J, carbon green). The ferricyanide ion and Trp–His adduct are shown with carbon colored magenta. (b) Binding of ferricyanide (magenta) in OS1 of the W396A:FECN structure (6I3K, carbon light blue). One water molecule (shown as red sphere, in two alternative positions) connects ferricyanide and His398. Interacting residues are marked. Distances are given in Ångströms. If values differ in chain A and B, they are given in parentheses for chain B of the corresponding structure. T1Cu is shown as orange sphere. The composite omit electron density map (2mFo-DFc) is shown as grey mesh and contoured at 1.0 σ level around the ferricyanide ion at the bottom of each panel. The map was calculated using Phenix⁶⁷. Anomalous difference Fourier is shown as red mesh and contoured at 2.5 σ level around iron. Molecular graphics were created using PyMOL (Schrödinger, LLC).