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. 2013 Jul 31;22(10):1306–1312. doi: 10.1002/pro.2317

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Published by Wiley-Blackwell. © 2013 The Protein Society

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Population analysis of Tyr298 dihedral angle. (A) Normalized probability of the side chain dihedral angle shows two states (inward and outward) sampled in the HDAC3¹² simulations. (B) Cartoon representation of HDAC3 from the HDAC3:IP4:DAD (black) and apo (green) simulations are superimposed to highlight the two Tyr298 conformations. An arbitrary acetyllysine peptide substrate was docked into the active site to show the functional relevance of the inward Tyr298 conformation (hydrogen atoms are not shown).

Inline graphic — Population analysis of Tyr298 dihedral angle. (A) Normalized probability of the side chain dihedral angle shows two states (inward and outward) sampled in the HDAC3¹² simulations. (B) Cartoon representation of HDAC3 from the HDAC3:IP4:DAD (black) and apo (green) simulations are superimposed to highlight the two Tyr298 conformations. An arbitrary acetyllysine peptide substrate was docked into the active site to show the functional relevance of the inward Tyr298 conformation (hydrogen atoms are not shown).