PDBe 1fpn

X-ray diffraction
2.6Å resolution

HUMAN RHINOVIRUS SEROTYPE 2 (HRV2)

Released:
Source organism: Human rhinovirus A2
Primary publication:
Structure of human rhinovirus serotype 2 (HRV2).
J. Mol. Biol. 300 1179-94 (2000)
PMID: 10903863

Function and Biology Details

Reactions catalysed:
NTP + H(2)O = NDP + phosphate. 
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 the picornavirus polyprotein. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
hetero 240-mer (preferred)
hetero tetramer
hetero 20-mer
hetero 24-mer
hetero 60-mer
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Capsid protein VP1 Chain: 1
Molecule details ›
Chain: 1
Length: 289 amino acids
Theoretical weight: 32.92 KDa
Source organism: Human rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 568-856; Coverage: 13%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP2 Chain: 2
Molecule details ›
Chain: 2
Length: 261 amino acids
Theoretical weight: 29.01 KDa
Source organism: Human rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 70-330; Coverage: 12%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP3 Chain: 3
Molecule details ›
Chain: 3
Length: 237 amino acids
Theoretical weight: 26.11 KDa
Source organism: Human rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 331-567; Coverage: 11%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP4 Chain: 4
Molecule details ›
Chain: 4
Length: 68 amino acids
Theoretical weight: 7.36 KDa
Source organism: Human rhinovirus A2
UniProt:
  • Canonical: P04936 (Residues: 2-69; Coverage: 3%)
Sequence domains: Picornavirus coat protein (VP4)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: I222
Unit cell:
a: 308.68Å b: 352.98Å c: 380.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 not available not available