› 6c2n

X-ray diffraction
1.8Å resolution

Crystal structure of HCV NS3/4A double mutant variant Y56H/D168A in complex with danoprevir

Released:
DOI: 10.2210/pdb6c2n/pdb
Model geometry
Fit model/data
PDB entry 6c2n coloured by chain, front view.
PDB entry 6c2n coloured by chain, side view.
PDB entry 6c2n coloured by chain, top view.
Source organism: hepatitis C virus genotype 1a
Entry authors: Matthew AN, Schiffer CA

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NS4A COFACTOR-NS3 PROTEIN CHIMERA Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.43 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8DG50 (Residues: 1013-1026, 1029-1208; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 1 x SO4
Ligand TSV 1 x TSV
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 59.964Å b: 55.355Å c: 58.891Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.19
Expression system: Escherichia coli BL21(DE3)

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