5lv2

X-ray diffraction
2.29Å resolution

Crystal structure of mouse CARM1 in complex with inhibitor LH1246

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-194407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 361 amino acids
Theoretical weight: 40.85 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9WVG6 (Residues: 130-487; Coverage: 59%)
Gene names: Carm1, Prmt4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 98.684Å b: 74.832Å c: 206.639Å
α: 90° β: 90.53° γ: 90°
R-values:
R R work R free
0.207 0.205 0.238
Expression system: Spodoptera frugiperda