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. 2022 Sep 5;13:5232. doi: 10.1038/s41467-022-32822-y

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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 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. 2 — a Side view (left) and extracellular view (right) of the FPR1-fMIFL structure. The receptor is shown as surface and cartoon, colored in cyan. The ligand fMIFL is shown as sphere with carbons in pink. b Slab view (light gray) of the binding cavity of fMIFL in FPR1. fMIFL assumes an N-terminus-in pose circled in red dashed line. c Side view of the binding pocket of FPR1-fMIFL structure. The receptor is shown as cartoon and colored in marine blue. The ligand fMIFL is shown as licorice with carbons in pink. Hydrogen bonds formed of R201^5.38XXXR205^5.42 motif with the N-formyl group, carbonyl groups of fMet in fMIFL, indicated in dash line. The residues of FPR1 within 4.5 Å to the atoms of fMIFL are shown in cyan licorice. d Extracellular (top) view of the FPR1-fMIFL structure. Red dashed lines indicate polar interactions between D106^3.33, the R201^5.38XXXR205^5.42 motif, and fMet in fMIFL. e, f Local density map of the ligand fMIFL and residues of FPR1 nearby the formyl group (CHO), viewed from two different angles.