1uzg

X-ray diffraction
3.5Å resolution

CRYSTAL STRUCTURE OF THE DENGUE TYPE 3 VIRUS ENVELOPE PROTEIN

Released:

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Envelope protein E Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 43.17 KDa
Source organism: Dengue virus 3
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P27915 (Residues: 281-672; Coverage: 12%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer : NEW Components: NAG, FUL, BMA
Carbohydrate polymer : NEW Components: NAG, FUL, MAN
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 52.855Å b: 68.631Å c: 270.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.286 0.284 0.324
Expression system: Drosophila melanogaster