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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-138281 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein
Molecule details ›
Chain: L
Length: 220 amino acids
Theoretical weight: 24.42 KDa
Source organism: Mus musculus
UniProt:
Sequence domains:
Structure domains: Immunoglobulins
Length: 220 amino acids
Theoretical weight: 24.42 KDa
Source organism: Mus musculus
UniProt:
- Canonical:
Q52L64 (Residues: 21-240; Coverage: 100%)
Sequence domains:
Structure domains: Immunoglobulins
Ig-like domain-containing protein
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.59 KDa
Source organism: Mus musculus
UniProt:
Sequence domains:
Structure domains: Immunoglobulins
Length: 218 amino acids
Theoretical weight: 23.59 KDa
Source organism: Mus musculus
UniProt:
- Canonical: Q505N9 (Residues: 20-126, 127-238; Coverage: 48%)
Sequence domains:
Structure domains: Immunoglobulins
Capsid protein VP2
Molecule details ›
Chain: P
Length: 16 amino acids
Theoretical weight: 1.71 KDa
Source organism: rhinovirus A2
UniProt:
Length: 16 amino acids
Theoretical weight: 1.71 KDa
Source organism: rhinovirus A2
UniProt:
- Canonical: P04936 (Residues: 225-239; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup:
P212121
