PDBe 6ffa

X-ray diffraction
1.5Å 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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Leader protease Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P03305 (Residues: 29-195; Coverage: 7%)
Ubiquitin-like protein ISG15 Chain: B
Molecule details ›
Chain: B
Length: 78 amino acids
Theoretical weight: 8.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05161 (Residues: 79-155; Coverage: 47%)
Gene names: G1P2, ISG15, UCRP
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 114.188Å b: 40.352Å c: 58.052Å
α: 90° β: 91.81° γ: 90°
R-values:
R R work R free
0.166 0.165 0.186
Expression system: Escherichia coli