4nwk

X-ray diffraction
1.62Å resolution

Crystal structure of hepatis c virus protease (ns3) complexed with bms-605339 aka n-(tert-butoxycarbonyl)-3-me thyl-l-valyl-(4r)-n-((1r,2s)-1-((cyclopropylsulfonyl)carba moyl)-2-vinylcyclopropyl)-4-((6-methoxy-1-isoquinolinyl)ox y)-l-prolinamide

Released:

Function and Biology Details

Reactions catalysed:
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
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'.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HCV NS3 1a Protease Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.26 KDa
Source organism: hepatitis C virus genotype 1a
Expression system: Escherichia coli
UniProt:
  • Canonical: A8DG50 (Residues: 1013-1026, 1031-1208; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21212
Unit cell:
a: 43.197Å b: 103.852Å c: 45.298Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.213
Expression system: Escherichia coli