5tbi

X-ray diffraction
2.29Å resolution

Crystal structure of mouse CARM1 in complex with inhibitor LH1427

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

Assembly composition:
homo tetramer (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: 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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 74.494Å b: 98.029Å c: 205.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.228
Expression system: Spodoptera frugiperda