Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
3C protease and peptide (preferred)
PDBe Complex ID:
PDB-CPX-111797 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
3C protease
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.06 KDa
Source organism: Coxsackievirus A16
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 190 amino acids
Theoretical weight: 21.06 KDa
Source organism: Coxsackievirus A16
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
C8CIL7 (Residues: 1-183; Coverage: 28%)
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007
Spacegroup:
P43212
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
