› 3wst

X-ray diffraction
2.39Å resolution

Crystal structure of C.elegans PRMT7 in complex with SAH(P31)

Released:
DOI: 10.2210/pdb3wst/pdb
PDB entry 3wst coloured by chain, front view.
PDB entry 3wst coloured by chain, side view.
PDB entry 3wst coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.
Hasegawa M, Toma-Fukai S, Kim JD, Fukamizu A, Shimizu T
FEBS Lett 588 1942-8 (2014)
PMID: 24726727

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195047 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 7 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Length: 655 amino acids
Theoretical weight: 74.09 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9XW42 (Residues: 1-647; Coverage: 100%)
Gene names: W06D4.4, pmrt-2, prmt-7
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SAH 18 x SAH
Ligand PO4 18 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P31
Unit cell:
a: 190.703Å b: 190.703Å c: 373.088Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.234 0.303
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
10 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