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:
Structure analysis Details
Assemblies composition:
Assembly name:
Serine protease/Helicase NS3 (preferred)
PDBe Complex ID:
PDB-CPX-139306 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease subunit NS2B
Molecule details ›
Chains: A, C
Length: 50 amino acids
Theoretical weight: 5.38 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
Length: 50 amino acids
Theoretical weight: 5.38 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P06935 (Residues: 1419-1463; Coverage: 1%)
Serine protease/Helicase NS3
Molecule details ›
Chains: B, D
Length: 198 amino acids
Theoretical weight: 21.37 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
Structure domains:
Length: 198 amino acids
Theoretical weight: 21.37 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
- Canonical: P06935 (Residues: 1502-1685; Coverage: 5%)
Structure domains:
