PDBe 2bhg

X-ray diffraction
1.9Å resolution

3C protease from type A10(61) foot-and-mouth disease virus

Released:

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Picornain 3C Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 22.96 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P03306 (Residues: 1650-1856; Coverage: 9%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: R3
Unit cell:
a: 141.589Å b: 141.589Å c: 43.677Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.245
Expression system: Escherichia coli