› 3lon

X-ray diffraction
2.2Å resolution

HCV NS3-4a protease domain with ketoamide inhibitor narlaprevir

Released:
DOI: 10.2210/pdb3lon/pdb
PDB entry 3lon coloured by chain, front view.
PDB entry 3lon coloured by chain, side view.
PDB entry 3lon coloured by chain, top view.
Source organisms:
Entry author: Prongay AJ

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163744 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Genome polyprotein Chains: A, C
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ELS8 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
KK-NS4a(21-39)-KK Chains: B, D
Molecule details ›
Chains: B, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand NNA 1 x NNA
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R32
Unit cell:
a: 224.392Å b: 224.392Å c: 75.331Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.269
Expression systems:
  • Escherichia coli
  • Not provided

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