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. 2023 Oct 30;13:18610. doi: 10.1038/s41598-023-45428-1

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© The Author(s) 2023

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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Stability analysis from MD simulations. The RMSF profile (a) shows that in the L3-35A, the helix 96–111 and the surrounding structures present a high degree of instability compared to the other enzymes. In the structural comparison (b, PnFPOX:green, AnFPOX:pink and L3-35A:blue), this helix (circled black) shows also a different fold compared to the other two enzymes. The instability and different structural arrangement could be due to design operated on L3-35A, which removed part of the helix blocking the tunnel (c, circled red). These removed residues were facing the helix 96–111 in the parental enzymes and were making stabilizing interactions, which could explain why helix 96–111 is unstable in L3-35A, possibly leading to its lower activity (d, color coded by RMSF, where blue represents lower RMSF and green–red the regions with higher RMSF). Comparison of RMSF and structure of PnFPOX (green), AnFPOX (pink) and L3-35A (blue).