PDBe 5dwq

X-ray diffraction
2.36Å resolution

Crystal structure of CARM1, sinefungin, and methylated H3 peptide (R17)


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:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-arginine methyltransferase CARM1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 349 amino acids
Theoretical weight: 39.62 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: Q86X55 (Residues: 134-479; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:
Histone H3.3 Chains: F, G
Molecule details ›
Chains: F, G
Length: 20 amino acids
Theoretical weight: 1.92 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P84243 (Residues: 14-31; Coverage: 13%)
Gene names: H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 75.424Å b: 98.404Å c: 208.369Å
α: 90° β: 90° γ: 90°
R R work R free
0.211 0.208 0.257
Expression systems:
  • Spodoptera frugiperda
  • Not provided