CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family Genome polyprotein

Enzyme Information

3.4.22.29
Picornain 2A.
based on mapping to UniProt P04936
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.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P04936
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.
3.4.22.28
Picornain 3C.
based on mapping to UniProt P04936
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P04936
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.

UniProtKB Entries (1)

P04936
POLG_HRV2
Human rhinovirus A2
Genome polyprotein

PDB Structure

PDB 1CQQ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
Matthews, D.A., Dragovich, P.S., Webber, S.E., Fuhrman, S.A., Patick, A.K., Zalman, L.S., Hendrickson, T.F., Love, R.A., Prins, T.J., Marakovits, J.T., Zhou, R., Tikhe, J., Ford, C.E., Meador, J.W., Ferre, R.A., Brown, E.L., Binford, S.L., Brothers, M.A., DeLisle, D.M., Worland, S.T.
Proc.Natl.Acad.Sci.USA