3m5o

X-ray diffraction
1.6Å resolution

Crystal structure of HCV NS3/4A protease in complex with N-terminal product 5A5B

Released:

Function and Biology Details

Reactions catalysed:
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-108607 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NS3/4A Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 21.49 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8DG50 (Residues: 1013-1017, 1018-1208; Coverage: 7%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
TEDVVCC peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 794 Da
Source organism: hepatitis C virus genotype 1a
Expression system: Not provided
UniProt:
  • Canonical: B3TKQ3 (Residues: 2414-2420; Coverage: 0%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P21
Unit cell:
a: 47.272Å b: 58.885Å c: 67.058Å
α: 90° β: 99.22° γ: 90°
R-values:
R R work R free
0.182 0.18 0.226
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided