› 6arj

X-ray diffraction
1.92Å resolution

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183245 (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: 349 amino acids
Theoretical weight: 39.62 KDa
Source organism: Homo sapiens
Expression system: Insect cell expression vector pTIE1
UniProt:
  • Canonical: Q86X55 (Residues: 134-479; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SAH 4 x SAH
Ligand BW4 4 x BW4
Ligand GOL 5 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21212
Unit cell:
a: 75.164Å b: 98.802Å c: 208.293Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.212
Expression system: Insect cell expression vector pTIE1

Quick links

Citations

20 review citations

Epigenetic modifications of histones in cancer.
Zhao et al. (2019)
19 more

3 mentions without citation

Identification of a CARM1 Inhibitor with Potent In Vitro and In Vivo Activity in Preclinical Models of Multiple Myeloma.
Drew et al. (2017)
2 more