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. 2022 Sep 28;12:16232. doi: 10.1038/s41598-022-20671-0

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© The Author(s) 2022

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 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/.

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Proximal P450 surface. (a) Positively charged residues in the lanosterol-bound M. capsulatus CYP51 molecule. The ribbon of helix K (306–318) is colored in dim grey, the meander (370–385) is in black. The heme and lanosterol are shown as black and cyan stick models, respectively. K99 (colored in black) is not exposed to the surface, its side chain retains the H-bond with the heme ring D propionate. (b–f) Electrostatic potential mapped onto the surface of bacterial (b–d) versus eukaryotic microsomal (e,f) and mitochondrial P450s (g,h). (b) M. capsulatus CYP51 [7SNM], (c) Tepidiphilus thermophiles CYP116B46 (P450_TT, 6LAA), (d) M. tuberculosis CYP51 [1E9X], (e) T. cruzi CYP51 [6FMO], (f) human CYP51 [6UEZ], (g) human CYP11A1 [P450scc, 3N9Y], (h) CYP11B2 [7M8I]. Red for positive and blue for negative charge, white for neutral. The view of the superimposed structures is the same as in (a).