4h9j

X-ray diffraction
1.6Å resolution

Crystal structure of N-terminal protease (Npro) of classical swine fever virus.

Released:

Function and Biology Details

Reactions catalysed:
Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hog cholera virus Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 17.29 KDa
Source organism: Classical swine fever virus - Alfort/187
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q68871 (Residues: 18-168; Coverage: 4%)
Sequence domains: Pestivirus Npro endopeptidase C53
Structure domains: Pestivirus Npro endopeptidase C53, interaction domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21212
Unit cell:
a: 60.133Å b: 65.398Å c: 33.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.208
Expression system: Escherichia coli BL21