› 5dst

X-ray diffraction
2.96Å resolution

Crystal structure of human PRMT8 in complex with SAH

Released:
DOI: 10.2210/pdb5dst/pdb
PDB entry 5dst coloured by chain, front view.
PDB entry 5dst coloured by chain, side view.
PDB entry 5dst coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel helical assembly in arginine methyltransferase 8.
Toma-Fukai S, Kim JD, Park KE, Kuwabara N, Shimizu N, Krayukhina E, Uchiyama S, Fukamizu A, Shimizu T
J Mol Biol 428 1197-1208 (2016)
PMID: 26876602

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-192529 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 8 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 332 amino acids
Theoretical weight: 38.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NR22 (Residues: 68-394; Coverage: 83%)
Gene names: HRMT1L3, HRMT1L4, PRMT8
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SAH 15 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: C2
Unit cell:
a: 199.983Å b: 130.943Å c: 294.377Å
α: 90° β: 106.48° γ: 90°
R-values:
R R work R free
0.225 0.224 0.26
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanisms and Inhibitors of Histone Arginine Methylation.
Fulton et al. (2018)
11 other articles

3 mentions without citation

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