2v7e

X-ray diffraction
2.7Å resolution

Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-194406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 346 amino acids
Theoretical weight: 39.1 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9WVG6 (Residues: 145-490; Coverage: 57%)
Gene names: Carm1, Prmt4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 74.146Å b: 98.018Å c: 206.915Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.276
Expression system: Spodoptera frugiperda