› 1a1v

X-ray diffraction
2.2Å resolution

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

Released:
DOI: 10.2210/pdb1a1v/pdb
PDB entry 1a1v coloured by chain, front view.
PDB entry 1a1v coloured by chain, side view.
PDB entry 1a1v coloured by chain, top view.
Source organism: Hepatitis C virus (isolate H)
Primary publication:
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.
Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR
Structure 6 89-100 (1998)
PMID: 9493270

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113387 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chain: A
Molecule details ›
Chain: A
Length: 476 amino acids
Theoretical weight: 51.36 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Escherichia coli
UniProt:
  • Canonical: P27958 (Residues: 1193-1659; Coverage: 16%)
Sequence domains: Flavivirus DEAD domain
Structure domains:
DNA (5'-D(*UP*UP*UP*UP*UP*UP*UP*U)-3') Chain: B
Molecule details ›
Chain: B
Length: 8 nucleotides
Theoretical weight: 2.28 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 73.1Å b: 117.5Å c: 63.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.287
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

70 review citations

Structure and mechanism of helicases and nucleic acid translocases.
Singleton et al. (2007)
69 more

42 mentions without citation

Computational methods in drug discovery.
Sliwoski et al. (2014)
41 more