› 4qqn

X-ray diffraction
2.08Å resolution

Protein arginine methyltransferase 3 in complex with compound MTV044246

Released:
DOI: 10.2210/pdb4qqn/pdb
PDB entry 4qqn coloured by chain, front view.
PDB entry 4qqn coloured by chain, side view.
PDB entry 4qqn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).
Kaniskan HÜ, Eram MS, Zhao K, Szewczyk MM, Yang X, Schmidt K, Luo X, Xiao S, Dai M, He F, Zang I, Lin Y, Li F, Dobrovetsky E, Smil D, Min SJ, Lin-Jones J, Schapira M, Atadja P, Li E, Barsyte-Lovejoy D, Arrowsmith CH, Brown PJ, Liu F, Yu Z, Vedadi M, Jin J
J Med Chem 61 1204-1217 (2018)
PMID: 29244490

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

4 bound ligands:
Ligand 3BQ 1 x 3BQ
Ligand GOL 1 x GOL
Ligand CL 1 x CL
Ligand UNX 12 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 70.319Å b: 70.319Å c: 172.918Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.212
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Methylation Status of the Epigenome: Its Emerging Role in the Regulation of Tumor Angiogenesis and Tumor Growth, and Potential for Drug Targeting.
Pirola et al. (2018)
5 more

3 mentions without citation

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