PDBe 1qol

X-ray diffraction
3Å resolution

Function and Biology Details

Reactions catalysed:
NTP + H(2)O = NDP + phosphate. 
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-. 
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. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leader protease Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 173 amino acids
Theoretical weight: 19.78 KDa
Source organism: Foot-and-mouth disease virus (strain O1)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03305 (Residues: 29-125, 127-201; Coverage: 7%)
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 65.43Å b: 101.56Å c: 276.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.258 0.314
Expression system: Escherichia coli BL21(DE3)