› 6arv

X-ray diffraction
2Å 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

3 bound ligands:
Ligand SAH 4 x SAH
Ligand BW7 4 x BW7
Ligand GOL 11 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21212
Unit cell:
a: 75.23Å b: 99.12Å c: 208.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.232
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

2 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)
1 more