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:

Function and Biology Details

Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (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:
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