4u01

X-ray diffraction
2.8Å resolution

HCV NS3/4A serine protease in complex with 6570

Released:
Entry authors: Parsy CC, Alexandre F-R, Brandt G, Caillet C, Chaves D, Derock M, Gloux D, Griffon Y, Lallos LB, Leroy F, Liuzzi M, Loi A-G, Mayes B, Moulat L, Moussa A, Chiara M, Roques V, Rosinovsky E, Seifer M, Stewart A, Wang J, Standring D, Surleraux D

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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'.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protease NS2 Chains: A, B, C, D, E, F, G, H, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, J
Length: 203 amino acids
Theoretical weight: 21.46 KDa
Source organism: Hepatitis C virus (isolate Con1)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WMX2 (Residues: 1026-1206; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
HCV_NS4a domain-containing protein Chains: K, L, M, N, O, P, Q, T, U
Molecule details ›
Chains: K, L, M, N, O, P, Q, T, U
Length: 16 amino acids
Theoretical weight: 1.69 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
UniProt:
  • Canonical: F0UY39 (Residues: 21-34; Coverage: 26%)
Gene name: NS4A

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 150.034Å b: 174.363Å c: 133.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.233 0.29
Expression system: Escherichia coli