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. 2022 Apr 9;21:58. doi: 10.1186/s12934-022-01777-6

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© The Author(s) 2022

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — Substrate, product tunnel and FAD-binding site in OhySa. A OhySa in light orange cartoon representation and the predicted substrate, product and FAD cavities in surface representation in yellow and green. The substrate/product channel from the exterior of the protein towards the FAD is shown in green and numbered “3”. The cavity with bound FAD is depicted in yellow and numbered with “2”. A side channel in vicinity of the FAD cavity is labelled with “3”. The tunnels were calculated with Caver 3.0 [62]. FAD is shown in black stick representation. Oleic acid (PDB ID: 7kaz; [47]) is shown in light green stick representation; 10-HSA bound to OhySa (PDB ID: 7kaz; [47]) is shown in dark blue stick representation as well as linoleic acid bound to OhyLa (PDB ID: 4ia6; [26]) is shown in light violet stick representation; Dashed box displays magnification area as shown in B. B Magnification of dashed box in A with the protein omitted. The ligands linoleic acid, oleic acid and polyethylene glycol are depicted as in A. The ligands guide the substrate channel from the distal end of the channel to the proximal catalytic cleft close to the FAD