Crystal structure of mouse CARM1 in complex with histone H3_13-31 K18

Structure

x-ray diffraction · 4 distinct chains · 29% helix, 35% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 4 copies · chains A, E, B, F, C, G, D, H
• QVR · (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol · ligand · 4 copies · chains A, E, B, F, C, G, D, H

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

15 interfaces between chains.

• C–D · 1952 Ų buried · 29 hydrogen bonds · protein-protein
• A–B · 1943 Ų buried · 26 hydrogen bonds · protein-protein
• D–H · 799 Ų buried · 11 hydrogen bonds · protein-protein
• A–E · 793 Ų buried · 12 hydrogen bonds · protein-protein
• B–F · 786 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (covalent ligand).

Compared structures

• 7OS4 · Crystal structure of mouse CARM1 in complex with histone H3_13-31 K18 · 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 B against A, TM-score 0.99

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 P68433
• Elsewhere: RCSB PDB 7OS4 · PDBe 7OS4 · UniProt Q9WVG6 · UniProt P68433