CATH Classification

Domain Context

CATH Clusters

Superfamily Picornavirus coat protein VP4
Functional Family

Enzyme Information

3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P03300
NTP + H(2)O = NDP + phosphate.
-!- The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. -!- Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD. -!- The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
3.4.22.29
Picornain 2A.
based on mapping to UniProt P03300
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
-!- From entero- and rhinoviruses. -!- Smaller than the homologous virus picornain 3C. -!- Belongs to peptidase family C3.
3.4.22.28
Picornain 3C.
based on mapping to UniProt P03300
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.
-!- From entero-, rhino-, aphto- and cardioviruses. -!- Larger than the homologous virus picornain 2A. -!- Belongs to peptidase family C3.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P03300
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.

UniProtKB Entries (1)

P03300
POLG_POL1M
Human poliovirus 1 Mahoney
Genome polyprotein

PDB Structure

PDB 1PO2
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Ligand-induced conformational changes in poliovirus-antiviral drug complexes.
Hiremath, C.N., Filman, D.J., Grant, R.A., Hogle, J.M.
Acta Crystallogr.,Sect.D