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:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero 180-mer (preferred)
Assembly name:
Polyprotein, capsid protein VP2 (preferred)
PDBe Complex ID:
PDB-CPX-125105 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Polyprotein, capsid protein VP1
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.09 KDa
Source organism: Coxsackievirus A16
UniProt:
Structure domains: Jelly Rolls
Length: 297 amino acids
Theoretical weight: 33.09 KDa
Source organism: Coxsackievirus A16
UniProt:
- Canonical:
I3W9E1 (Residues: 566-862; Coverage: 14%)
Structure domains: Jelly Rolls
Polyprotein, capsid protein VP2
Molecule details ›
Chain: B
Length: 254 amino acids
Theoretical weight: 27.59 KDa
Source organism: Coxsackievirus A16
UniProt:
Structure domains: Jelly Rolls
Length: 254 amino acids
Theoretical weight: 27.59 KDa
Source organism: Coxsackievirus A16
UniProt:
- Canonical: I3W9E1 (Residues: 70-323; Coverage: 12%)
Structure domains: Jelly Rolls
Polyprotein, capsid protein VP3
Molecule details ›
Chain: C
Length: 242 amino acids
Theoretical weight: 26.65 KDa
Source organism: Coxsackievirus A16
UniProt:
Structure domains: Jelly Rolls
Length: 242 amino acids
Theoretical weight: 26.65 KDa
Source organism: Coxsackievirus A16
UniProt:
- Canonical: I3W9E1 (Residues: 324-565; Coverage: 11%)
Structure domains: Jelly Rolls
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
DIAMOND BEAMLINE I03
Spacegroup:
I222
