7qph

X-ray diffraction
1.9Å resolution

Crystal structure of mouse CARM1 in complex with histone H3_22-31 K27 acetylated

Released:
Model geometry
Fit model/data
Source organism: Mus musculus
Entry authors: Marechal N, Cura V, Troffer-Charlier N, Bonnefond L, Cavarelli J

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:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-159469 (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: 361 amino acids
Theoretical weight: 40.85 KDa
Source organism: Mus musculus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
  • Canonical: Q9WVG6 (Residues: 130-487; Coverage: 59%)
Gene names: Carm1, Prmt4
Sequence domains:
Histone H3.1 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 10 amino acids
Theoretical weight: 1.04 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P68433 (Residues: 23-32; Coverage: 7%)
Gene names: H3.1-221, H3.1-291, H3.1-I, H3a, H3c1, H3c10, H3c11, H3c8, H3g, H3h, H3i, Hist1h3a, Hist1h3g, Hist1h3h, Hist1h3i

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 75.343Å b: 99.184Å c: 208.443Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.21
Expression systems:
  • Spodoptera aff. frugiperda 1 BOLD-2017
  • Not provided