Crystal structure of CARM1 in complex with inhibitor AA183

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 36% strand (DSSP).

Ligands and binding sites

• KXW · (2~{S})-4-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[3-(pyridin-2-ylamino)propyl]amino]-2-azanyl-butanoic acid · ligand · 4 copies · chains A, B, C, D
• GOL · Glycerol · additive · 2 copies · chains B, C

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• B–C · 1897 Ų buried · 24 hydrogen bonds · protein-protein
• A–D · 1863 Ų buried · 25 hydrogen bonds · protein-protein
• A–B · 648 Ų buried · 9 hydrogen bonds · protein-protein
• B–D · 164 Ų buried · 2 hydrogen bonds · protein-protein
• A–C · 159 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 6S79 · Crystal structure of CARM1 in complex with inhibitor AA183 · 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 C 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 6S79 · PDBe 6S79 · UniProt Q86X55