Crystal structure of mouse CARM1 in complex with ligand LH1561BR

Structure

x-ray diffraction · 4 distinct chains · 30% helix, 37% strand (DSSP).

Ligands and binding sites

• SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, D
• LHF · 5-[[2-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]ethylamino]methyl]-4-azanyl-1-[2-(4-bromanylphenoxy)ethyl]pyrimidin-2-one · ligand · 2 copies · chains B, 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, 5 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1941 Ų buried · 26 hydrogen bonds · protein-protein
• C–D · 1934 Ų buried · 26 hydrogen bonds · protein-protein
• B–D · 738 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 191 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 181 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 5LV3 · Crystal structure of mouse CARM1 in complex with ligand LH1561Br · 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 5LV3 · PDBe 5LV3 · UniProt Q9WVG6