› 3ua4

X-ray diffraction
3Å resolution

Crystal Structure of Protein Arginine Methyltransferase PRMT5

Released:
DOI: 10.2210/pdb3ua4/pdb
PDB entry 3ua4 coloured by chain, front view.
PDB entry 3ua4 coloured by chain, side view.
PDB entry 3ua4 coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Structural insights into protein arginine symmetric dimethylation by PRMT5.
Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM
Proc Natl Acad Sci U S A 108 20538-43 (2011)
PMID: 22143770

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-155487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 745 amino acids
Theoretical weight: 84.75 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P46580 (Residues: 1-734; Coverage: 100%)
Gene names: C34E10.5, prmt-5, tag-251
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 100.56Å b: 129.49Å c: 149.719Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.288
Expression system: Escherichia coli

Quick links

Citations

20 review citations

The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.
Stopa et al. (2015)
19 more

6 mentions without citation

Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.
Tewary et al. (2019)
5 more