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. 2017 Nov 21;7:15898. doi: 10.1038/s41598-017-16123-9

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© The Author(s) 2017

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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Sequence alignment of Saccharomyces cerevisiae lanosterol 14-α demethylase with six Mucorales CYP51s. R. arrhizus F1 (n = 17) and F5 CYP51s (n = 3), R. microsporus F1 and F5 CYP51s (n = 13 for both LDMs) and M. circinelloides F1 and F5 CYP51s (n = 18 for both LDMs) were aligned against S. cerevisiae CYP51 using T-coffee (Expresso)⁶¹. Residues within 4 Å of voriconazole in the structure S. cerevisiae CYP51 (PDBID: 5HS1⁴³) are highlighted in green. Those highlighted in red correspond to resistance mutations in CYP51 F5. The V to A substitution is shown in blue. Helices from the voriconazole CYP51 complex are shown above the alignment in gray and the heme coordinating cysteine is shown in yellow. The final two residues of the S. cerevisiae sequence are not shown. MH, Membrane-associated helix; TMD, transmembrane domain.