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X-ray diffraction
2.75Å resolution

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN: NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND PYRROLIDINE-5,5-TRANSLACTAM INHIBITOR

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 tetramer (preferred)
PDBe Complex ID:
PDB-CPX-128771 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 21.26 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
UniProt:
  • Canonical: P26664 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Hepatitis C virus Non-structural protein NS4a domain-containing protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepacivirus C
Expression system: Not provided
UniProt:
  • Canonical: O39914 (Residues: 4-24; Coverage: 24%)
Gene name: NS4a/b
Sequence domains: Hepatitis C virus non-structural protein NS4a

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: R32
Unit cell:
a: 224.082Å b: 224.082Å c: 75.694Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.234
Expression systems:
  • Escherichia coli
  • Not provided