2xhv

X-ray diffraction
1.9Å resolution

HCV-J4 NS5B Polymerase Point Mutant Orthorhombic Crystal Form

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131655 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 579 amino acids
Theoretical weight: 64.64 KDa
Source organism: Hepatitis C virus isolate HC-J4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O92972 (Residues: 2420-2989; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 105.74Å b: 107.69Å c: 133.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.2
Expression system: Escherichia coli BL21(DE3)