3dpr

X-ray diffraction
3.5Å resolution

Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3

Released:
Model geometry
Fit model/data

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 300-mer (preferred)
PDBe Complex ID:
PDB-CPX-138285 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Capsid protein VP1 Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.92 KDa
Source organism: rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 568-856; Coverage: 13%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP2 Chain: B
Molecule details ›
Chain: B
Length: 261 amino acids
Theoretical weight: 29.01 KDa
Source organism: rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 70-330; Coverage: 12%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP3 Chain: C
Capsid protein VP4 Chain: D
Very low-density lipoprotein receptor Chain: E

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P43212
Unit cell:
a: 498.117Å b: 498.117Å c: 658.425Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.426 0.425 0.441
Expression system: Escherichia coli