Crystal structure of mouse CARM1 in complex with inhibitor SA0649

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 36% strand (DSSP).

Ligands and binding sites

• 6D2 · 5'-{[(3S)-3-amino-3-carboxypropyl](3-carbamimidamidopropyl)amino}-5'-deoxyadenosine · ligand · 4 copies · chains A, B, C, D
• DXE · 1,2-dimethoxyethane · ligand · 4 copies · chains A, B, C
• EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, D
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, D, B, C
• PGE · Triethylene glycol · additive · chains A
• PE8 · 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol · 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.

• A–B · 1922 Ų buried · 25 hydrogen bonds · protein-protein
• C–D · 1893 Ų buried · 26 hydrogen bonds · protein-protein
• B–D · 838 Ų buried · 10 hydrogen bonds · protein-protein
• B–C · 184 Ų buried · 2 hydrogen bonds · protein-protein
• A–D · 180 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 5ISE · Crystal structure of mouse CARM1 in complex with inhibitor SA0649 · 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 5ISE · PDBe 5ISE · UniProt Q9WVG6