2z83

X-ray diffraction
1.8Å resolution

Crystal Structure of Catalytic Domain of Japanese Encephalitis Virus NS3 Helicase/Nucleoside Triphosphatase at a Resolution 1.8

Released:
Source organism: Japanese encephalitis virus
Entry author: Yamashita T

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 459 amino acids
Theoretical weight: 51.68 KDa
Source organism: Japanese encephalitis virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P27395 (Residues: 1685-2123; Coverage: 13%)
Sequence domains: Flavivirus DEAD domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 59.062Å b: 68.024Å c: 65.219Å
α: 90° β: 116.87° γ: 90°
R-values:
R R work R free
0.202 0.199 0.249
Expression system: Escherichia coli