› 1f3l

X-ray diffraction
2.03Å resolution

CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3

Released:
DOI: 10.2210/pdb1f3l/pdb
PDB entry 1f3l coloured by chain, front view.
PDB entry 1f3l coloured by chain, side view.
PDB entry 1f3l coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.
Zhang X, Zhou L, Cheng X
EMBO J 19 3509-19 (2000)
PMID: 10899106

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130702 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 3 Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.21 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O70467 (Residues: 208-528; Coverage: 61%)
Gene names: Hrmt1l3, Prmt3
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SAH 1 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, NSLS BEAMLINE X26C, OTHER
Spacegroup: P43212
Unit cell:
a: 70.91Å b: 70.91Å c: 177.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.262
Expression system: Escherichia coli

Quick links

Citations

34 review citations

Arginine methylation an emerging regulator of protein function.
Bedford et al. (2005)
33 more

24 mentions without citation

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