Function and Biology Details
Reactions catalysed:
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA +S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H(+).
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaacan be either Arg or Lys and Yaa can be either Ser or Ala.
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate+ phosphate + H(+).
ATP + H2O = ADP + phosphate + H(+).
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Serine protease subunit NS2B (preferred)
PDBe Complex ID:
PDB-CPX-174291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 48.95 KDa
Source organism: Zika virus
Expression system: Escherichia coli
UniProt:
Length: 435 amino acids
Theoretical weight: 48.95 KDa
Source organism: Zika virus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q32ZE1 (Residues: 1681-2115; Coverage: 13%)
