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.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assemblies composition:
Assembly name:
Protease 3C (preferred)
PDBe Complex ID:
PDB-CPX-140226 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protease 3C
Molecule details ›
Chain: A
Length: 217 amino acids
Theoretical weight: 23.9 KDa
Source organism: Hepatovirus A
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 217 amino acids
Theoretical weight: 23.9 KDa
Source organism: Hepatovirus A
Expression system: Escherichia coli
UniProt:
- Canonical:
P08617 (Residues: 1520-1736; Coverage: 10%)
Structure domains: Trypsin-like serine proteases
Protease 3C
Molecule details ›
Chain: B
Length: 217 amino acids
Theoretical weight: 23.95 KDa
Source organism: Hepatovirus A
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 217 amino acids
Theoretical weight: 23.95 KDa
Source organism: Hepatovirus A
Expression system: Escherichia coli
UniProt:
- Canonical: P08617 (Residues: 1520-1736; Coverage: 10%)
Structure domains: Trypsin-like serine proteases
