Skip to main content
. Author manuscript; available in PMC: 2022 Jun 24.
Published in final edited form as: J Med Chem. 2021 May 17;64(12):8510–8522. doi: 10.1021/acs.jmedchem.1c00430

Figure 2.

Figure 2.

Molecular mechanism for the association of the PHF1 Tudor domain with UNC6641 (PDB ID: 7LKY). (a) The electrostatic surface potential of the PHF1 Tudor domain. Bound UNC6641 is colored green, and the phenyl substituent of K4 is indicated as Lig. (b) The 2Fo-Fc electron-density map of UNC6641 contoured at 1 σ shown as a gray mesh. (c) Structure of the PHF1 Tudor domain in complex with UNC6641. The PHF1 Tudor domain is shown as a gray ribbon, UNC6641 is shown as green sticks, and the protein residues interacting with UNC6641 are shown as gray sticks (except for W41, Y47, F65, and F71, which are colored yellow). The hydrogen bonds are indicated by yellow dashed lines. (d) Zoomed-in view of the UNC6641 binding site. (e) Overlay of the structures of the of PHF1 Tudor domain in complex with the H3K36me3 peptide (purple sticks) (PDB ID: 4HCZ) and UNC6641 (green sticks).