› 5tbj

X-ray diffraction
2.32Å resolution

Crystal structure of mouse CARM1 in complex with inhibitor LH1452

Released:
DOI: 10.2210/pdb5tbj/pdb
PDB entry 5tbj coloured by chain, front view.
PDB entry 5tbj coloured by chain, side view.
PDB entry 5tbj coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Hijacking DNA methyltransferase transition state analogues to produce chemical scaffolds for PRMT inhibitors.
Halby L, Marechal N, Pechalrieu D, Cura V, Franchini DM, Faux C, Alby F, Troffer-Charlier N, Kudithipudi S, Jeltsch A, Aouadi W, Decroly E, Guillemot JC, Page P, Ferroud C, Bonnefond L, Guianvarc'h D, Cavarelli J, Arimondo PB
Philos Trans R Soc Lond B Biol Sci 373 (2018)
PMID: 29685976

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194407 (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:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand LHD 4 x LHD
Ligand PEG 4 x PEG
Ligand EDO 11 x EDO
Ligand DXE 1 x DXE
Ligand PG6 1 x PG6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 74.844Å b: 99.2Å c: 207.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.237
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

The Roles of Host 5-Methylcytosine RNA Methyltransferases during Viral Infections.
Wnuk et al. (2020)
9 other articles

3 mentions without citation

Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.
Tewary et al. (2019)
2 more