4k8b

X-ray diffraction
2.8Å resolution

Crystal structure of HCV NS3/4A protease complexed with inhibitor

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate
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
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-150810 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S29 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.05 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0ZNA6 (Residues: 1-181; Coverage: 100%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.21 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 1678-1689; Coverage: 0%)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P3221
Unit cell:
a: 76.182Å b: 76.182Å c: 169.206Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.203 0.232
Expression system: Escherichia coli