2yol

X-ray diffraction
3.2Å resolution

West Nile Virus NS2B-NS3 protease in complex with 3,4- dichlorophenylacetyl-Lys-Lys-GCMA

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 24.6 KDa
Source organism: West Nile virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06935 (Residues: 1420-1466, 1502-1671; Coverage: 6%)
Sequence domains: Peptidase S7, Flavivirus NS3 serine protease
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P3221
Unit cell:
a: 118.7Å b: 118.7Å c: 66.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.207
Expression system: Escherichia coli BL21(DE3)