1raj

X-ray diffraction
2.5Å resolution

Poliovirus Polymerase with a 68 residue N-terminal truncation

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 44.79 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Escherichia coli
UniProt:
  • Canonical: P03300 (Residues: 1817-2209; Coverage: 18%)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 87.71Å b: 87.71Å c: 107.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.242 0.262
Expression system: Escherichia coli