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
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serine protease NS3 and RNA (preferred)
PDBe Complex ID:
PDB-CPX-174141 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Serine protease NS3
Molecule details ›
Chains: A, B
Length: 451 amino acids
Theoretical weight: 51.37 KDa
Source organism: Dengue virus 4 Thailand/0348/1991
Expression system: Escherichia coli
UniProt:
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 451 amino acids
Theoretical weight: 51.37 KDa
Source organism: Dengue virus 4 Thailand/0348/1991
Expression system: Escherichia coli
UniProt:
- Canonical:
Q2YHF0 (Residues: 1645-2092; Coverage: 13%)
Structure domains: P-loop containing nucleotide triphosphate hydrolases
