5wx1

X-ray diffraction
2.35Å resolution

The closed-conformation crystal structure of the full-length pestivirus NS3 with its NS4A protease cofactor segment

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Autoprotease p20 Chain: A
Molecule details ›
Chain: A
Length: 733 amino acids
Theoretical weight: 81.54 KDa
Source organism: Classical swine fever virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5U8X5 (Residues: 1590-2272; Coverage: 18%)
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P42212
Unit cell:
a: 111.084Å b: 111.084Å c: 139.032Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.25
Expression system: Escherichia coli BL21(DE3)