› 4y34

X-ray diffraction
2.7Å resolution

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3D polymerase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 53.17 KDa
Source organism: Coxsackievirus B3
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5UEA2 (Residues: 1724-2185; Coverage: 21%)
Sequence domains: Viral RNA-dependent RNA polymerase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 45Z 1 x 45Z
Ligand SO4 5 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43212
Unit cell:
a: 74.62Å b: 74.62Å c: 288.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.241
Expression system: Escherichia coli

Quick links

Citations

15 review citations

RNA Dependent RNA Polymerases: Insights from Structure, Function and Evolution.
Venkataraman et al. (2018)
14 more

1 mention without citation

The RNA template channel of the RNA-dependent RNA polymerase as a target for development of antiviral therapy of multiple genera within a virus family.
van der Linden et al. (2015)