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
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212810 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Envelope protein E
Molecule details ›
Chain: E
Length: 402 amino acids
Theoretical weight: 43.42 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 402 amino acids
Theoretical weight: 43.42 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9Q6P4 (Residues: 291-692; Coverage: 12%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 4.2.2
Spacegroup:
P21212
Expression systems:
- Escherichia coli
- Mus musculus
