Crystal structure of mouse CARM1 in complex with inhibitor LH1452

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 37% strand (DSSP).

Ligands and binding sites

• LHD · 2-[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]ethyl-[[4-azanyl-1-(methoxymethyl)-2-oxidanylidene-pyrimidin-5-yl]methyl]azanium · ligand · 4 copies · chains A, B, C, D
• DXE · 1,2-dimethoxyethane · ligand · chains A
• EDO · 1,2-ethanediol · additive · 11 copies · chains A, D, B, C
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B, C
• PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains B

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.

• C–D · 1926 Ų buried · 25 hydrogen bonds · protein-protein
• A–B · 1910 Ų buried · 28 hydrogen bonds · protein-protein
• B–D · 744 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 218 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 195 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 5TBJ · Crystal structure of mouse CARM1 in complex with inhibitor LH1452 · the same entry in another collection · chain C against C, 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 5TBJ · PDBe 5TBJ · UniProt Q9WVG6