7x38

Electron Microscopy
3.52Å resolution

Cryo-EM structure of Coxsackievirus B1 empty particle in complex with nAb 8A10 (CVB1-E:8A10)

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero 300-mer (preferred)
PDBe Complex ID:
PDB-CPX-224635 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
8A10 light chain Chain: L
Molecule details ›
Chain: L
Length: 108 amino acids
Theoretical weight: 11.95 KDa
Source organism: Mus musculus
8A10 heavy chain Chain: H
Molecule details ›
Chain: H
Length: 118 amino acids
Theoretical weight: 13.32 KDa
Source organism: Mus musculus
VP1 Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.21 KDa
Source organism: Coxsackievirus B1
UniProt:
  • Canonical: W8GTF7 (Residues: 1-278; Coverage: 100%)
Sequence domains: picornavirus capsid protein
VP2 Chain: B
Molecule details ›
Chain: B
Length: 263 amino acids
Theoretical weight: 29.12 KDa
Source organism: Coxsackievirus B1
UniProt:
  • Canonical: A0A2S0RQC2 (Residues: 70-332; Coverage: 12%)
Sequence domains: picornavirus capsid protein
VP3 Chain: C
Molecule details ›
Chain: C
Length: 238 amino acids
Theoretical weight: 26.33 KDa
Source organism: Coxsackievirus B1
UniProt:
  • Canonical: L7UV52 (Residues: 333-570; Coverage: 11%)
Sequence domains: picornavirus capsid protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.52Å
Relevant EMDB volumes: EMD-32981