Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

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

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 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/.

PMC Copyright notice

Binding mode of the CYP51 substrate is conserved across phylogeny. (a) The 2Fo-Fc electron density map (at 2σ) for lanosterol, the heme, and the H-bond forming residues, Y186 and L324, in the structure of M. capsulatus CYP51. (b) Sterol substrates bound in the active center of bacterial (M. capsulatus—cyan, and eukaryotic CYP51s (human—rosy-brown, and T. cruzi—salmon). The residues preceding the β1-4 strand (L324, I379, and M358) whose main chain carbonyl oxygen forms the H-bond with the sterol hydroxyl are colored correspondingly. The distances and the H-bonds are depicted as magenta and green dashes, respectively.