3lkz

X-ray diffraction
2Å resolution

Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-192974 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase NS5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 36.74 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Q6P4 (Residues: 2529-2828; Coverage: 9%)
Gene names: GP1, MZ11_60484gpGP1, MZ11_60553gpGP1
Sequence domains: FtsJ-like methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SFG 2 x SFG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 39.363Å b: 65.74Å c: 77.119Å
α: 112.01° β: 102.65° γ: 90.19°
R-values:
R R work R free
0.229 0.229 0.269
Expression system: Escherichia coli