› 3bsc

X-ray diffraction
2.65Å resolution

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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 578 amino acids
Theoretical weight: 64.35 KDa
Source organism: Hepatitis C virus (isolate BK)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 2420-2989; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand 2PD 2 x 2PD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 85.336Å b: 106.55Å c: 127.273Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.277
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recent advances in drug discovery of benzothiadiazine and related analogs as HCV NS5B polymerase inhibitors.
Das et al. (2011)
1 more

4 mentions without citation

Multiple virtual screening approaches for finding new hepatitis C virus RNA-dependent RNA polymerase inhibitors: structure-based screens and molecular dynamics for the pursue of new poly pharmacological inhibitors.
Elhefnawi et al. (2012)
3 more