Function and Biology Details
Reactions catalysed:
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:
hetero trimer (preferred)
Assembly name:
3D polymerase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-192987 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
2 distinct RNA molecules
Macromolecules (3 distinct):
3D polymerase
Molecule details ›
Chain: A
Length: 476 amino acids
Theoretical weight: 53.52 KDa
Source organism: Foot and mouth disease virus C
Expression system: Escherichia coli BL21
UniProt:
Structure domains:
Length: 476 amino acids
Theoretical weight: 53.52 KDa
Source organism: Foot and mouth disease virus C
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9QCE3 (Residues: 1858-2327; Coverage: 20%)
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 14-ID-B
Spacegroup:
P41212
Expression systems:
- Escherichia coli BL21
- Not provided
