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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 catalytic residues of PhaC_Cs-CAT. (a) A close-up view of the catalytic site of PhaC_Cs-CAT. The catalytic triad residues (orange) comprise Cys291, His477 and Asp447, with a hydrogen bond between His477 and Asp447. The catalytic center Cys291 is located at the nucleophilic elbow sandwiched with nonpolar residues Phe290 and Val292 (green). Hydrogen bonds are indicated by broken lines. (b) Overlay of the catalytic triad of PhaC_Cs-CAT (orange) onto human gastric lipase (1HLG in green). (c) Overlay of the active site with the catalytic triad of PhaC_Cs-CAT (orange) onto those of PhaC_Cn-CAT (5T6O in yellow; 5HZ2 in magenta). The imidazole ring of the His residue of PhaC_Cn-CAT (magenta) is flipped from the other two.