› 1orh

X-ray diffraction
2.64Å resolution

Structure of the Predominant Protein Arginine Methyltransferase PRMT1

Released:
DOI: 10.2210/pdb1orh/pdb
PDB entry 1orh coloured by chain, front view.
PDB entry 1orh coloured by chain, side view.
PDB entry 1orh coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.
Zhang X, Cheng X
Structure 11 509-20 (2003)
PMID: 12737817

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 domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-162355 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein arginine N-methyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 40.57 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63009 (Residues: 1-353; Coverage: 100%)
Gene names: Hrmt1l2, Prmt1
Sequence domains: Methyltransferase domain
Structure domains:
Substrate peptide Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 869 Da
Source organism: Rattus norvegicus
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SAH 1 x SAH
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P4122
Unit cell:
a: 87.84Å b: 87.84Å c: 144.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.248
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

38 review citations

Protein arginine methylation in mammals: who, what, and why.
Bedford et al. (2009)
37 more

10 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
9 more