2oqb

X-ray diffraction
1.69Å resolution

Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-175446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 117 amino acids
Theoretical weight: 12.85 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q4AE70 (Residues: 28-140; Coverage: 17%)
Gene names: Carm1, Prmt4
Sequence domains: Coactivator-associated arginine methyltransferase 1 N terminal
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41212
Unit cell:
a: 46.127Å b: 46.127Å c: 201.325Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.205 0.255
Expression system: Escherichia coli BL21