Crystal structure of CARM1 in complex with inhibitor UM305

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 37% strand (DSSP).

Ligands and binding sites

• KY8 · (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-azanylpropyl-[3-(pyrimidin-2-ylamino) propyl]amino]methyl]oxolane-3,4-diol · ligand · 4 copies · chains A, B, C, D
• GOL · Glycerol · additive · 3 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–C · 1862 Ų buried · 25 hydrogen bonds · protein-protein
• B–D · 1826 Ų buried · 23 hydrogen bonds · protein-protein
• C–D · 725 Ų buried · 10 hydrogen bonds · protein-protein
• B–C · 182 Ų buried · 2 hydrogen bonds · protein-protein
• A–D · 173 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 6S74 · Crystal structure of CARM1 in complex with inhibitor UM305 · the same entry in another collection · chain D against D, TM-score 1.00
• Q86X55 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q86X55) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q86X55
• Elsewhere: RCSB PDB 6S74 · PDBe 6S74 · UniProt Q86X55