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.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
NTP + H(2)O = NDP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Capsid protein VP1 (preferred)
PDBe Complex ID:
PDB-CPX-136760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein VP1
Molecule details ›
Chain: A
Length: 20 amino acids
Theoretical weight: 1.97 KDa
Source organism: Foot-and-mouth disease virus (strain A12)
Expression system: Not provided
UniProt:
Length: 20 amino acids
Theoretical weight: 1.97 KDa
Source organism: Foot-and-mouth disease virus (strain A12)
Expression system: Not provided
UniProt:
- Canonical:
P03308 (Residues: 865-883; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
torsion angle dynamics
Expression system: Not provided
