Fig. 3: Crystal structure of ASH1L SET in complex with AS-5. | Nature Communications

Fig. 3: Crystal structure of ASH1L SET in complex with AS-5.

From: Discovery of first-in-class inhibitors of ASH1L histone methyltransferase with anti-leukemic activity

Fig. 3: Crystal structure of ASH1L SET in complex with AS-5.

a Overall structure of ASH1L-AS-5 complex with 2Fo-Fc electron density map for AS-5 contoured at the 1σ level. Protein is shown as ribbon with autoinhibitory loop in magenta and AS-5 shown in sticks with green carbons. b ASH1L residues involved in hydrophobic contacts with AS-5 shown in sticks and transparent surfaces (gray) and SAM is shown in sticks with the blue surface. Hydrogen bonds and chalcogen bonds are shown as dashed lines. Color-coding: AS-5 carbons (green), protein and SAM carbons (gray), oxygens (red), nitrogen (blue), sulfur (yellow). c Details of internal pocket in ASH1L (shown as semi-transparent surface) and binding mode of AS-5 (shown in sticks with green carbons). Selected residues in the ASH1L binding site are shown as sticks with color coding is as in panel (c). Hydrogen bonds and chalcogen bonds are shown as dashed lines with distances in Å. d Superposition of ASH1L structure (PDB code 4YNM with salmon carbons) on the structure of ASH1L-AS-5 complex (protein with gray carbons and AS-5 with green carbons).

Back to article page