3rc4

X-ray diffraction
1.5Å resolution

Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease

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-151110 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protease NS2 Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.49 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27958 (Residues: 1026-1208; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
TIR domain-containing adapter molecule 1 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q8IUC6 (Residues: 360-372; Coverage: 2%)
Gene names: PRVTIRB, TICAM1, TRIF

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 53.9Å b: 58.146Å c: 61.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.215
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided