Crystal structure of mouse CARM1 in complex with inhibitor SA0707

Structure

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

Ligands and binding sites

• 6D6 · 5'-{[(3S)-3-amino-3-carboxypropyl](3-aminopropyl) amino}-5'-deoxyadenosine · ligand · 4 copies · chains A, B, C, D
• DXE · 1,2-dimethoxyethane · ligand · 3 copies · chains A, B
• M2M · 1-methoxy-2-(2-methoxyethoxy)ethane · ligand · chains A
• EDO · 1,2-ethanediol · additive · 18 copies · chains A, B, C, D
• PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, D
• PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains A

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1957 Ų buried · 29 hydrogen bonds · protein-protein
• C–D · 1918 Ų buried · 29 hydrogen bonds · protein-protein
• B–D · 809 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 221 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 211 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 5ISG · Crystal structure of mouse CARM1 in complex with inhibitor SA0707 · 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 5ISG · PDBe 5ISG · UniProt Q9WVG6