› 5egs

X-ray diffraction
2.15Å 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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 376 amino acids
Theoretical weight: 42.07 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q96LA8 (Residues: 1-375; Coverage: 100%)
Gene names: HRMT1L6, PRMT6
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SAH 4 x SAH
Ligand 5NR 6 x 5NR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 77.157Å b: 135.616Å c: 83.086Å
α: 90° β: 98.91° γ: 90°
R-values:
R R work R free
0.202 0.201 0.246
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

A patent review of arginine methyltransferase inhibitors (2010-2018).
Li et al. (2019)
4 more

6 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
5 more