› 3smq

X-ray diffraction
2Å resolution

Crystal structure of protein arginine methyltransferase 3

Released:
DOI: 10.2210/pdb3smq/pdb
PDB entry 3smq coloured by chain, front view.
PDB entry 3smq coloured by chain, side view.
PDB entry 3smq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An allosteric inhibitor of protein arginine methyltransferase 3.
Siarheyeva A, Senisterra G, Allali-Hassani A, Dong A, Dobrovetsky E, Wasney GA, Chau I, Marcellus R, Hajian T, Liu F, Korboukh I, Smil D, Bolshan Y, Min J, Wu H, Zeng H, Loppnau P, Poda G, Griffin C, Aman A, Brown PJ, Jin J, Al-Awar R, Arrowsmith CH, Schapira M, Vedadi M
Structure 20 1425-35 (2012)
PMID: 22795084

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 3 Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 38.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60678 (Residues: 211-531; Coverage: 61%)
Gene names: HRMT1L3, PRMT3
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand TDU 1 x TDU
Ligand CL 1 x CL
Ligand UNX 10 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P43212
Unit cell:
a: 70.649Å b: 70.649Å c: 171.977Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.215
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

15 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
14 more