6sk7

Electron Microscopy
2.9Å 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:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero 240-mer (preferred)
PDBe Complex ID:
PDB-CPX-505241 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Capsid protein VP1 Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 33.29 KDa
Source organism: Human rhinovirus 89 ATCC VR-1199
UniProt:
  • Canonical: P07210 (Residues: 575-872; Coverage: 14%)
Sequence domains: picornavirus capsid protein
Capsid protein VP2 Chain: B
Molecule details ›
Chain: B
Length: 267 amino acids
Theoretical weight: 29.42 KDa
Source organism: Human rhinovirus 89 ATCC VR-1199
UniProt:
  • Canonical: P07210 (Residues: 70-336; Coverage: 12%)
Sequence domains: picornavirus capsid protein
Capsid protein VP3 Chain: C
Molecule details ›
Chain: C
Length: 238 amino acids
Theoretical weight: 26.33 KDa
Source organism: Human rhinovirus 89 ATCC VR-1199
UniProt:
  • Canonical: P07210 (Residues: 337-574; Coverage: 11%)
Sequence domains: picornavirus capsid protein
VP4/VP2 protein Chain: D
Molecule details ›
Chain: D
Length: 69 amino acids
Theoretical weight: 7.46 KDa
Source organism: Human rhinovirus 89 ATCC VR-1199
UniProt:
  • Canonical: D3KZ50 (Residues: 1-69; Coverage: 49%)
Sequence domains: Picornavirus coat protein (VP4)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-10222