4u01

X-ray diffraction
2.8Å resolution

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-123274 (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:
Hepatitis C virus Non-structural protein 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