› 3emb

X-ray diffraction
2.3Å resolution

Wesselsbron virus Methyltransferase in complex with AdoMet and 7MeGpppG

Released:
DOI: 10.2210/pdb3emb/pdb
PDB entry 3emb coloured by chain, front view.
PDB entry 3emb coloured by chain, side view.
PDB entry 3emb coloured by chain, top view.
Source organism: Wesselsbron virus
Primary publication:
Recognition of RNA cap in the Wesselsbron virus NS5 methyltransferase domain: implications for RNA-capping mechanisms in Flavivirus.
Bollati M, Milani M, Mastrangelo E, Ricagno S, Tedeschi G, Nonnis S, Decroly E, Selisko B, de Lamballerie X, Coutard B, Canard B, Bolognesi M
J Mol Biol 385 140-52 (2009)
PMID: 18976670

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
mRNA cap 0-1 NS5-type MT domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 34.19 KDa
Source organism: Wesselsbron virus
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VX01 (Residues: 1-275; Coverage: 100%)
Sequence domains: FtsJ-like methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
2 bound ligands:
Ligand GTG 1 x GTG
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 37.236Å b: 61.297Å c: 128.012Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.166 0.229
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Structural insights into SARS-CoV-2 proteins.
Arya et al. (2021)
11 more

5 mentions without citation

Structure and functionality in flavivirus NS-proteins: perspectives for drug design.
Bollati et al. (2010)
4 more