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. 2017 Jul 13;7:5312. doi: 10.1038/s41598-017-05509-4

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© The Author(s) 2017

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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The channel of the active site of PhaC_Cs. (a) A close-up view of the β9-α5-β10 segment forming part of the active site of PhaC_Cs-CAT. Ala479 of PhaC_Cs is located at α5 helix, where His477 of the catalytic triad is also located. Asp368 of the LID region stabilizes α5 helix by forming hydrogen bonds to the main chain amide groups of Ile478 and Ala479 residues which form the helix. Ala479 corresponds to Ala510 of PhaC_Cn. (b) A view of the channel at the active site of PhaC_Cs-CAT. Trp392 of PhaC_Cs is located in the αC helix of the CAP subdomain and faces Site B of the channel where a water cluster is present. Tyr412 and Ile413 are located in the αD helix of the CAP subdomain. Tyr412 projects into Site A of the channel, while Ile413 forms a hydrophobic core with other aliphatic residues.