Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- Helicase superfamily 1/2, ATP-binding domain
- Hepatitis C virus, NS3 protease
- Helicase, C-terminal domain-like
- Non-structural protein NS3-like, DEAD box helicase, flavivirus
- Peptidase S1, PA clan, chymotrypsin-like fold
- Peptidase S1, PA clan
- Heat shock protein 70kD, C-terminal domain superfamily
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Serine protease/helicase NS3 (preferred)
PDBe Complex ID:
PDB-CPX-150815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease/helicase NS3
Molecule details ›
Chains: A, B
Length: 666 amino acids
Theoretical weight: 70.87 KDa
Source organism: Hepatitis C virus (isolate BK)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains:
Length: 666 amino acids
Theoretical weight: 70.87 KDa
Source organism: Hepatitis C virus (isolate BK)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P26663 (Residues: 1013-1025, 1029-1657; Coverage: 21%)
Structure domains:
