Crystal structure of mouse CARM1 in complex with ligand SA684

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 35% strand (DSSP).

Ligands and binding sites

• DXE · 1,2-dimethoxyethane · ligand · 5 copies · chains A, B
• 6YB · (2~{S})-4-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(2-carbamimidamidoethyl)amino]-2-azanyl-butanoic acid · ligand · 4 copies · chains A, B, C, D
• EDO · 1,2-ethanediol · additive · 8 copies · chains A, D, B, C
• PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, C
• P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains B

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 1996 Ų buried · 29 hydrogen bonds · protein-protein
• C–D · 1911 Ų buried · 28 hydrogen bonds · protein-protein
• B–D · 851 Ų buried · 10 hydrogen bonds · protein-protein
• A–D · 196 Ų buried · 2 hydrogen bonds · protein-protein
• B–C · 188 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 5LKJ · Crystal structure of mouse CARM1 in complex with ligand SA684 · 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 B 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 5LKJ · PDBe 5LKJ · UniProt Q9WVG6