PDBe 1or8

X-ray diffraction
2.35Å resolution

Structure of the Predominant protein arginine methyltransferase PRMT1

Released:

Function and Biology Details

Reaction catalysed:
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine. 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero pentamer (preferred)
homo dimer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Substrate peptide Chains: B, C, D, E
Molecule details ›
Chains: B, C, D, E
Length: 19 amino acids
Theoretical weight: 1.67 KDa
Source organism: Synthetic construct
Expression system: Not provided
Protein arginine N-methyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 39.27 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63009 (Residues: 14-353; Coverage: 96%)
Gene names: Hrmt1l2, Prmt1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P4122
Unit cell:
a: 86.5Å b: 86.5Å c: 142.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.254
Expression systems:
  • Not provided
  • Escherichia coli