› 3ely

X-ray diffraction
2.4Å resolution

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 SAH 1 x SAH
2 bound ligands:
Ligand SO4 5 x SO4
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 49.715Å b: 66.436Å c: 91.055Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.256
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

2 mentions without citation

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