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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-208645 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein VP1
Molecule details ›
Chain: P
Length: 18 amino acids
Theoretical weight: 1.94 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Not provided
UniProt:
Length: 18 amino acids
Theoretical weight: 1.94 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Not provided
UniProt:
- Canonical:
P03300 (Residues: 665-682; Coverage: 1%)
Ig gamma-2A chain C region, membrane-bound form
Molecule details ›
Chain: H
Length: 220 amino acids
Theoretical weight: 23.48 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Length: 220 amino acids
Theoretical weight: 23.48 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical: P01865 (Residues: 1-99; Coverage: 25%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P6322
Expression system: Not provided
