› 4ryl

X-ray diffraction
2.1Å resolution

Human Protein Arginine Methyltransferase 3 in complex with 1-isoquinolin-6-yl-3-[2-oxo-2-(pyrrolidin-1-yl)ethyl]urea

Released:
DOI: 10.2210/pdb4ryl/pdb
PDB entry 4ryl coloured by chain, front view.
PDB entry 4ryl coloured by chain, side view.
PDB entry 4ryl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A potent, selective and cell-active allosteric inhibitor of protein arginine methyltransferase 3 (PRMT3).
Kaniskan HÜ, Szewczyk MM, Yu Z, Eram MS, Yang X, Schmidt K, Luo X, Dai M, He F, Zang I, Lin Y, Kennedy S, Li F, Dobrovetsky E, Dong A, Smil D, Min SJ, Landon M, Lin-Jones J, Huang XP, Roth BL, Schapira M, Atadja P, Barsyte-Lovejoy D, Arrowsmith CH, Brown PJ, Zhao K, Jin J, Vedadi M
Angew Chem Int Ed Engl 54 5166-70 (2015)
PMID: 25728001

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

2 bound ligands:
Ligand 3ZG 1 x 3ZG
Ligand UNX 2 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 70.691Å b: 70.691Å c: 173.559Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.232
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Arginine Methylation: The Coming of Age.
Blanc et al. (2017)
18 more

9 mentions without citation

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
8 more