4x41

X-ray diffraction
3.5Å resolution

Crystal Structure of Protein Arginine Methyltransferase PRMT8

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 41.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NR22 (Residues: 61-394; Coverage: 85%)
Gene names: HRMT1L3, HRMT1L4, PRMT8
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P2221
Unit cell:
a: 68.159Å b: 78.236Å c: 203.861Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.231 0.282
Expression system: Escherichia coli