› 7p2r

X-ray diffraction
2.3Å 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-180090 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 38.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6NZB1 (Residues: 34-378; Coverage: 91%)
Gene names: Hrmt1l6, Prmt6
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand 4R7 2 x 4R7
Ligand SAH 1 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-X
Spacegroup: P21
Unit cell:
a: 41.797Å b: 118.687Å c: 72.052Å
α: 90° β: 102.79° γ: 90°
R-values:
R R work R free
0.202 0.199 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Development of Potent and Selective Coactivator-Associated Arginine Methyltransferase 1 (CARM1) Degraders.
Xie et al. (2023)
3 more

1 mention without citation

Turning Nonselective Inhibitors of Type I Protein Arginine Methyltransferases into Potent and Selective Inhibitors of Protein Arginine Methyltransferase 4 through a Deconstruction-Reconstruction and Fragment-Growing Approach.
Iannelli et al. (2022)