4a1x

X-ray diffraction
1.9Å resolution

Co-Complex structure of NS3-4A protease with the inhibitory peptide CP5-46-A (Synchrotron data)

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-150805 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 21.39 KDa
Source organism: Hepatitis C virus subtype 1b
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26662 (Residues: 1678-1690, 1028-1206; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
CP5-46-A PEPTIDE Chains: C, D
Molecule details ›
Chains: C, D
Length: 21 amino acids
Theoretical weight: 2.3 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P61
Unit cell:
a: 93.32Å b: 93.32Å c: 82.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.182
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided