Fig. 4
From: Structural and functional specificity of H3K36 methylation
Conserved histone-interacting residues in the SET domain of SETD2. Asterisk (*) and white arrow in the figure, respectively, label the position of SETD2 β15 beta sheet and α6 helix to depict relative orientation of SETD2 crystalized structure in different sub-figures. A F1589, Y1604, F1606, F1668, and Y1671 (green) interact with G33-V35 (dark red) of the histone H3 peptide (red) via hydrogen bonding. B Key catalytic residues Tyr-1578, Met-1607, Phe-1664 and Tyr-1666 (green) of the SETD2 SET domain (yellow) surround the K36/M36 residues (dark red) of the histone H3 peptide (red). C Key auto-inhibitory residue R1670 (green) of the LIN loop (brown) in SETD2 SET domain (yellow) is in proximity to K36 (dark red) on histone H3 peptide (red). D E1636 and T1637 (green) interact with Y41 (dark red) of the histone H3 peptide (red) via hydrogen bonding. Pymol visualization is derived from the crystalized structure database in the Protein Data Bank entry 5V22 [160].