› 7puq

X-ray diffraction
2.09Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 360 amino acids
Theoretical weight: 40.79 KDa
Source organism: Mus musculus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
  • Canonical: Q9WVG6 (Residues: 130-486; Coverage: 59%)
Gene names: Carm1, Prmt4
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand 867 4 x 867
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21212
Unit cell:
a: 75.128Å b: 98.694Å c: 207.778Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.217
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017

Quick links

Citations

4 citation in other articles

Development of Potent and Selective Coactivator-Associated Arginine Methyltransferase 1 (CARM1) Degraders.
Xie et al. (2023)
3 more

1 mention without citation

Turning Nonselective Inhibitors of Type I Protein Arginine Methyltransferases into Potent and Selective Inhibitors of Protein Arginine Methyltransferase 4 through a Deconstruction-Reconstruction and Fragment-Growing Approach.
Iannelli et al. (2022)