› 4c04

X-ray diffraction
1.58Å resolution

Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with inhibitor

Released:
DOI: 10.2210/pdb4c04/pdb
PDB entry 4c04 coloured by chain, front view.
PDB entry 4c04 coloured by chain, side view.
PDB entry 4c04 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Functional insights from high resolution structures of mouse protein arginine methyltransferase 6.
Bonnefond L, Stojko J, Mailliot J, Troffer-Charlier N, Cura V, Wurtz JM, Cianférani S, Cavarelli J
J Struct Biol 191 175-83 (2015)
PMID: 26094878

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-180090 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 6 Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 42.32 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: Q6NZB1 (Residues: 1-378; Coverage: 100%)
Gene names: Hrmt1l6, Prmt6
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SFG 1 x SFG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: I41
Unit cell:
a: 78.835Å b: 78.835Å c: 118.472Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.151 0.185

Quick links

Citations

4 review citations

Biochemistry and regulation of the protein arginine methyltransferases (PRMTs).
Morales et al. (2016)
3 more

5 mentions without citation

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