PDBe 2a4g

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate
NTP + H(2)O = NDP + phosphate
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'.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease NS3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
UniProt:
  • Canonical: P26664 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
NS4a peptide Chains: B, D
Molecule details ›
Chains: B, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepatitis C virus subtype 1b
Expression system: Not provided
UniProt:
  • Canonical: Q9QP61 (Residues: 1676-1696; Coverage: 1%)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 224.392Å b: 224.392Å c: 75.334Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.265
Expression systems:
  • Escherichia coli
  • Not provided