5lv4

X-ray diffraction
1.66Å resolution

Crystal structure of mouse PRMT6 in complex with inhibitor LH1236

Released:

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 6 Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.6 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6NZB1 (Residues: 1-378; Coverage: 100%)
Gene names: Hrmt1l6, Prmt6
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: I41
Unit cell:
a: 79.851Å b: 79.851Å c: 119.738Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.188
Expression system: Escherichia coli