5lbv

X-ray diffraction
2.2Å resolution

Structural basis of zika and dengue virus potent antibody cross-neutralization

Released:

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-100082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Envelope protein E Chains: A, B
Molecule details ›
Chains: A, B
Length: 447 amino acids
Theoretical weight: 48.49 KDa
Source organism: Zika virus
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: A0A024B7W1 (Residues: 291-698; Coverage: 12%)
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2221
Unit cell:
a: 64.628Å b: 213.566Å c: 124.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.239
Expression system: Drosophila melanogaster