CARM1 in complex with EML736

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 36% strand (DSSP).

Ligands and binding sites

• LSK · methyl 6-[5-[[~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl]carbamimidoyl]amino]pentylcarbamoylamino]-4-oxidanyl-naphthalene-2-carboxylate · ligand · 4 copies · chains A, B, C, D
• EDO · 1,2-ethanediol · additive · 7 copies · chains A, B, D, C

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 1935 Ų buried · 27 hydrogen bonds · protein-protein
• C–D · 1910 Ų buried · 28 hydrogen bonds · protein-protein
• B–D · 760 Ų buried · 9 hydrogen bonds · protein-protein
• A–D · 182 Ų buried · 1 hydrogen bond · protein-protein
• B–C · 181 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

• 7PPQ · CARM1 in complex with EML736 · the same entry in another collection · chain D against D, TM-score 1.00
• Q9WVG6 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q9WVG6) · 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 Q9WVG6
• Elsewhere: RCSB PDB 7PPQ · PDBe 7PPQ · UniProt Q9WVG6