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. 2017 Jun 12;7:3228. doi: 10.1038/s41598-017-03417-1

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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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Comparison of Class I and Class IIa HDAC cavities. (A) Sequence alignment of residues within the catalytic site of class I (pink) and class IIa (blue) HDAC isozymes as shown. Residue numbering for HDAC4 is located on top. (B) Structural alignment of HDAC2 (green) and HDAC4 (brown) with different residues (boxes) are shown at designated positions. Blue circles highlight residue differences. (C) Stick model of class IIa isozymes are aligned with inhibitor A4291 (blue) docked from HDAC4. (D) The surface model of the HDAC4 active site is superimposed with inhibitor A4291 to show the relative cavity size. (E) Stick model of class I isozymes aligned with inhibitor A4291 (blue) docked from HDAC4. Enzymes are labeled as shown. (F) The surface model of HDAC2 (green stick model) is superimposed with inhibitor A4291 docked from HDAC4 (blue). Location of residue Y308 is indicated by red circle. Note the reduced space within the active site due to Y308. Zinc is indicated by grey sphere.