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:
monomeric (preferred)
Assembly name:
Serine protease NS3 (preferred)
PDBe Complex ID:
PDB-CPX-136776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.4 KDa
Source organism: Yellow fever virus
Expression system: Escherichia coli
UniProt:
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 440 amino acids
Theoretical weight: 49.4 KDa
Source organism: Yellow fever virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P03314 (Residues: 1670-2107; Coverage: 13%)
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P21
Expression system: Escherichia coli
