3knx

X-ray diffraction
2.65Å resolution

Function and Biology Details

Reactions catalysed:
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-190145 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
HCV NS3 Protease Chains: A, C
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepatitis C virus (isolate H77)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ELS8 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
HCV NS4a peptide Chains: B, D
Molecule details ›
Chains: B, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Not provided
UniProt:
  • Canonical: Q9ELS8 (Residues: 1678-1696; Coverage: 1%)
Sequence domains: Hepatitis C virus non-structural protein NS4a

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 223.587Å b: 223.587Å c: 75.282Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.169 0.263
Expression systems:
  • Escherichia coli
  • Not provided