2cxv

X-ray diffraction
1.4Å resolution

Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-Derived betaLactone: Selective Crystallization and High-resolution Structure of the His-102 Adduct

Released:

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.
NTP + H(2)O = NDP + phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146811 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.12 KDa
Source organism: Human hepatitis A virus Hu/Northern Africa/MBB/1978
Expression system: Escherichia coli
UniProt:
  • Canonical: P13901 (Residues: 1520-1738; Coverage: 10%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 44.249Å b: 56.022Å c: 80.649Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.166 0.188
Expression system: Escherichia coli