PDBe 1rgq

X-ray diffraction
2.9Å resolution

M9A HCV Protease complex with pentapeptide keto-amide inhibitor


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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 21.26 KDa
Source organism: Hepatitis C virus
Expression system: Escherichia coli
  • Canonical: P27958 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4a/b Chains: C, D
Molecule details ›
Chains: C, D
Length: 22 amino acids
Theoretical weight: 2.26 KDa
Source organism: Hepatitis C virus
Expression system: Not provided
  • Canonical: O39914 (Residues: 6-26; Coverage: 24%)
Gene name: NS4a/b

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 226.385Å b: 226.385Å c: 76.864Å
α: 90° β: 90° γ: 120°
R R work R free
0.279 0.279 0.312
Expression systems:
  • Escherichia coli
  • Not provided