› 6mvo

X-ray diffraction
1.95Å 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-150817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 562 amino acids
Theoretical weight: 62 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26664 (Residues: 2421-2982; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase

Ligands and Environments

2 bound ligands:
Ligand SO4 7 x SO4
Ligand K4P 2 x K4P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 53.225Å b: 61.202Å c: 91.773Å
α: 89.7° β: 86.98° γ: 80.92°
R-values:
R R work R free
0.218 0.217 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Boronic Acids and Their Derivatives in Medicinal Chemistry: Synthesis and Biological Applications.
Silva et al. (2020)
1 more

4 mentions without citation

Recent developments in the medicinal chemistry of single boron atom-containing compounds.
Song et al. (2021)
3 more

PDB-REDO

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