1oan

X-ray diffraction
2.75Å resolution

Crystal structure of the dengue 2 virus envelope protein

Released:
Source organism: Dengue virus 2
Primary publication:
A ligand-binding pocket in the dengue virus envelope glycoprotein.
Proc Natl Acad Sci U S A 100 6986-91 (2003)
PMID: 12759475

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
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]
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:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-146330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Envelope protein E Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 43.82 KDa
Source organism: Dengue virus 2
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P12823 (Residues: 281-674; Coverage: 12%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P3121
Unit cell:
a: 81.541Å b: 81.541Å c: 288.623Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.261 0.261 0.296
Expression system: Drosophila melanogaster