› 2qe2

X-ray diffraction
2.9Å resolution

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-189299 (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: 64.25 KDa
Source organism: Hepatitis C virus subtype 1b
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99AU2 (Residues: 2420-2989; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase

Ligands and Environments

1 bound ligand:
Ligand 452 2 x 452
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 70.835Å b: 70.878Å c: 251.653Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.279 0.279 0.296
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

2 mentions without citation

Inhibition of hepatitis C virus replication by Monascus pigment derivatives that interfere with viral RNA polymerase activity and the mevalonate biosynthesis pathway.
Sun et al. (2012)
1 more