Crystal structure of CARM1 in complex with inhibitor WH5C

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 37% strand (DSSP).

Ligands and binding sites

• KYE · (2~{S})-4-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(5-carbamimidamidopentyl)amino]-2-azanyl-butanoic acid · ligand · 4 copies · chains A, B, C, D
• GOL · Glycerol · additive · 7 copies · chains A, B, C, D

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

Pockets

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

Interfaces

5 interfaces between chains.

• B–D · 1931 Ų buried · 26 hydrogen bonds · protein-protein
• A–C · 1891 Ų buried · 27 hydrogen bonds · protein-protein
• C–D · 885 Ų buried · 13 hydrogen bonds · protein-protein
• A–D · 200 Ų buried · 2 hydrogen bonds · protein-protein
• B–C · 183 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

• 6S71 · Crystal structure of CARM1 in complex with inhibitor WH5C · the same entry in another collection · chain D against D, TM-score 1.00
• Q86X55 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q86X55) · a predicted model of the same protein · chain B 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 Q86X55
• Elsewhere: RCSB PDB 6S71 · PDBe 6S71 · UniProt Q86X55