Crystal structure of mouse CARM1 in complex with ligand P2C3S

Structure

x-ray diffraction · 5 distinct chains · 30% helix, 36% strand (DSSP).

Ligands and binding sites

• 8ZB · (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-propyl-oxolane-3,4-diol · ligand · 4 copies · chains B, F, A, E, C, G, D, H
• DXE · 1,2-dimethoxyethane · ligand · chains A
• SO4 · Sulfate ion · ion · chains A
• EDO · 1,2-ethanediol · additive · 7 copies · chains A, B, C, D
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, D, C, B
• 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, 8 with a druggability of 0.5 or more.

Interfaces

10 interfaces between chains.

• A–B · 1933 Ų buried · 25 hydrogen bonds · protein-protein
• C–D · 1896 Ų buried · 27 hydrogen bonds · protein-protein
• B–D · 765 Ų buried · 9 hydrogen bonds · protein-protein
• D–H · 675 Ų buried · 10 hydrogen bonds · protein-protein
• A–E · 645 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent (covalent ligand).

Compared structures

• 5LGQ · Crystal structure of mouse CARM1 in complex with ligand P2C3s · the same entry in another collection · chain H against H, 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
• Every structure of UniProt P11940
• Elsewhere: RCSB PDB 5LGQ · PDBe 5LGQ · UniProt Q9WVG6 · UniProt P11940