2whx

X-ray diffraction
2.2Å resolution

A second conformation of the NS3 protease-helicase from dengue virus

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
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.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 618 amino acids
Theoretical weight: 69.49 KDa
Source organism: Dengue virus 4
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YHF0 (Residues: 1475-2092; Coverage: 18%)
Sequence domains:
Structure domains:
Serine protease subunit NS2B Chain: C
Molecule details ›
Chain: C
Length: 14 amino acids
Theoretical weight: 1.56 KDa
Source organism: Dengue virus 4
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YHF0 (Residues: 1393-1406; Coverage: 0%)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC
Spacegroup: P21
Unit cell:
a: 52.42Å b: 87.72Å c: 75.779Å
α: 90° β: 92.9° γ: 90°
R-values:
R R work R free
0.23 0.228 0.272
Expression system: Escherichia coli