6lb1

Electron Microscopy
2.58Å resolution

Cryo-EM structure of echovirus 11 A-particle at pH 5.5

Released:

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)
PDBe Complex ID:
PDB-CPX-102663 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein VP1 Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 26.05 KDa
Source organism: Echovirus E11
UniProt:
  • Canonical: Q2LJ73 (Residues: 60-285; Coverage: 77%)
Sequence domains: picornavirus capsid protein
Capsid protein VP2 Chain: B
Molecule details ›
Chain: B
Length: 245 amino acids
Theoretical weight: 27.37 KDa
Source organism: Echovirus E11
UniProt:
  • Canonical: A0A0R5YS56 (Residues: 81-325; Coverage: 11%)
Sequence domains: picornavirus capsid protein
Capsid protein VP3 Chain: C
Molecule details ›
Chain: C
Length: 231 amino acids
Theoretical weight: 25.29 KDa
Source organism: Echovirus E11
UniProt:
  • Canonical: A8ILJ7 (Residues: 332-562; Coverage: 26%)
Sequence domains: picornavirus capsid protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.58Å
Relevant EMDB volumes: EMD-0867