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
Assemblies composition:
Assembly name:
Protease 3C (preferred)
PDBe Complex ID:
PDB-CPX-136767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.27 KDa
Source organism: Coxsackievirus B3
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 183 amino acids
Theoretical weight: 20.27 KDa
Source organism: Coxsackievirus B3
Expression system: Escherichia coli
UniProt:
- Canonical:
P03313 (Residues: 1541-1723; Coverage: 8%)
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSRRC BEAMLINE BL13B1
Spacegroup:
P21
Expression system: Escherichia coli
