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:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Capsid protein VP3 (preferred)
PDBe Complex ID:
PDB-CPX-136689 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 19.65 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Escherichia coli BL21
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 183 amino acids
Theoretical weight: 19.65 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P03300 (Residues: 1566-1748; Coverage: 8%)
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU200
Spacegroup:
P212121
Expression system: Escherichia coli BL21
