› 5tsk

Electron Microscopy
6.5Å resolution

Molecular Dynamics Flexible Fitting Model of Coxsackievirus A16 empty Procapsid VP1 Subunit

Released:
DOI: 10.2210/pdb5tsk/pdb
PDB entry 5tsk coloured by chain, front view.
PDB entry 5tsk coloured by chain, side view.
PDB entry 5tsk coloured by chain, top view.
Source organism: Coxsackievirus A16
Primary publication:
Structural alteration and surface modifi cation of coxsackievirus A16 capsids by beta-propiolactone treatment
Chen F, Ye X, Ku ZI, Kong Ll, Liu Q, Xu C, Cong Y, Huang Z
J. Virol. (2017)
Related structures: EMD-8325

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo 60-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
coxsackievirus A16 empty procapsid VP1 subunit Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.09 KDa
Source organism: Coxsackievirus A16
UniProt:
  • Canonical: A9LXZ4 (Residues: 566-862; Coverage: 14%)
Sequence domains: Picornavirus coat protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 6.5Å
Relevant EMDB volumes: EMD-8325

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