4hdh

X-ray diffraction
2.28Å resolution

Crystal Structure of viral RdRp in complex with ATP

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-150989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase NS5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 639 amino acids
Theoretical weight: 73.38 KDa
Source organism: Japanese encephalitis virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P27395 (Residues: 2799-3432; Coverage: 19%)
Sequence domains:
Structure domains: Flavivirus RNA-directed RNA polymerase, thumb domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 144.838Å b: 86.506Å c: 112.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.225 0.272
Expression system: Escherichia coli