3oyp

X-ray diffraction
2.76Å resolution

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-150802 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 187 amino acids
Theoretical weight: 19.75 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26662 (Residues: 1027-1213; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: C, D
Molecule details ›
Chains: C, D
Length: 16 amino acids
Theoretical weight: 1.69 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26662 (Residues: 1678-1691; Coverage: 1%)
Peptidomimetic inhibitor Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 677 Da

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P61
Unit cell:
a: 94.401Å b: 94.401Å c: 83.129Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.215 0.274
Expression system: Escherichia coli