› 5mz4

X-ray diffraction
3.05Å resolution

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 752 amino acids
Theoretical weight: 83.67 KDa
Source organism: Hog cholera virus (strain Alfort)
Expression system: Escherichia coli
UniProt:
  • Canonical: P19712 (Residues: 2293-2329, 1590-2280; Coverage: 19%)
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 127.211Å b: 168.839Å c: 98.495Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.233
Expression system: Escherichia coli

Quick links

Citations

6 review citations

RNA-virus proteases counteracting host innate immunity.
Lei et al. (2017)
5 more

1 mention without citation

Determination of Critical Requirements for Classical Swine Fever Virus NS2-3-Independent Virion Formation.
Dubrau et al. (2019)