Crystal structure of mouse CARM1 in complex with inhibitor SA0401

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 36% strand (DSSP).

Ligands and binding sites

• 6D5 · (2~{S})-4-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(3-azidopropyl)amino]-2-azanyl-butanoic acid · ligand · 4 copies · chains C, D, A, B
• DXE · 1,2-dimethoxyethane · ligand · 3 copies · chains C, A
• M2M · 1-methoxy-2-(2-methoxyethoxy)ethane · ligand · chains A
• NA · Sodium ion · metal · chains B
• EDO · 1,2-ethanediol · additive · 8 copies · chains C, D, A, B
• PEG · Di(hydroxyethyl)ether · additive · chains A
• PG4 · Tetraethylene glycol · 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, 5 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1982 Ų buried · 26 hydrogen bonds · protein-protein
• C–D · 1954 Ų buried · 28 hydrogen bonds · protein-protein
• D–B · 915 Ų buried · 10 hydrogen bonds · protein-protein
• C–B · 234 Ų buried · 3 hydrogen bonds · protein-protein
• D–A · 217 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 5ISA · Crystal structure of mouse CARM1 in complex with inhibitor SA0401 · the same entry in another collection · chain C against C, 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 5ISA · PDBe 5ISA · UniProt Q9WVG6