› 1ori

X-ray diffraction
2.5Å resolution

Structure of the predominant protein arginine methyltransferase PRMT1

Released:
DOI: 10.2210/pdb1ori/pdb
PDB entry 1ori coloured by chain, front view.
PDB entry 1ori coloured by chain, side view.
PDB entry 1ori 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:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-178988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 343 amino acids
Theoretical weight: 39.63 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63009 (Residues: 11-353; Coverage: 97%)
Gene names: Hrmt1l2, Prmt1
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P4122
Unit cell:
a: 88.27Å b: 88.27Å c: 145.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.263
Expression system: Escherichia coli

Quick links

Citations

36 review citations

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

25 mentions without citation

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