3j0b

Electron Microscopy
10.3Å resolution

cryo-EM reconstruction of West Nile virus

Released:
Source organism: West Nile virus
Primary publication:
Membrane curvature in flaviviruses.
J Struct Biol 183 86-94 (2013)
PMID: 23602814
Related structures: EMD-5296

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 180-mer (preferred)
PDBe Complex ID:
PDB-CPX-192977 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Envelope protein E Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 400 amino acids
Theoretical weight: 43.27 KDa
Source organism: West Nile virus
UniProt:
  • Canonical: Q9Q6P4 (Residues: 291-690; Coverage: 12%)
Gene names: GP1, MZ11_60484gpGP1, MZ11_60553gpGP1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 10.3Å
Relevant EMDB volumes: EMD-5296