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.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
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 VP4 (preferred)
PDBe Complex ID:
PDB-CPX-136755 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 22.52 KDa
Source organism: Foot-and-mouth disease virus (strain A10-61)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 209 amino acids
Theoretical weight: 22.52 KDa
Source organism: Foot-and-mouth disease virus (strain A10-61)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P03306 (Residues: 1649-1856; Coverage: 9%)
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SRS BEAMLINE PX10.1
Spacegroup:
P212121
Expression system: Escherichia coli BL21(DE3)
