3p8n

X-ray diffraction
1.9Å resolution

Crystal structure of HCV NS3/NS4A protease complexed with BI 201335

Released:

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-150801 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 19.66 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26662 (Residues: 1027-1206; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: C, D
Molecule details ›
Chains: C, D
Length: 17 amino acids
Theoretical weight: 1.82 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Not provided
UniProt:
  • Canonical: P26662 (Residues: 1678-1691; Coverage: 1%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P61
Unit cell:
a: 94.874Å b: 94.874Å c: 81.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.203 0.242
Expression systems:
  • Escherichia coli
  • Not provided