Crystal structure of mouse CARM1 in complex with inhibitor LH1236

Structure

x-ray diffraction · 3 distinct chains.

Ligands and binding sites

• 78K · (2~{R})-4-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[[4-azanyl-1-(methoxymethyl)-2-oxidanylidene-pyrimidin-5-yl]methyl]amino]-2-azanyl-butanoic acid · ligand · 2 copies · chains B, D
• M2M · 1-methoxy-2-(2-methoxyethoxy)ethane · ligand · chains A
• EDO · 1,2-ethanediol · additive · 17 copies · chains A, B, C, D
• PG4 · Tetraethylene glycol · additive · chains A, D

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

Compared structures

• 5TBH · Crystal structure of mouse CARM1 in complex with inhibitor LH1236 · the same entry in another collection · chain B against B, 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 5TBH · PDBe 5TBH · UniProt Q9WVG6