5lgp

X-ray diffraction
2.04Å resolution

Crystal structure of mouse CARM1 in complex with ligand P1C3s

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:
hetero octamer (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 frugiperda
UniProt:
  • Canonical: Q9WVG6 (Residues: 130-487; Coverage: 59%)
Gene names: Carm1, Prmt4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:
Polyadenylate-binding protein 1 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 13 amino acids
Theoretical weight: 1.3 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11940 (Residues: 447-458; Coverage: 2%)
Gene names: PAB1, PABP, PABP1, PABPC1, PABPC2

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 74.794Å b: 98.714Å c: 207.253Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.219
Expression systems:
  • Spodoptera frugiperda
  • Not provided