1sfk

X-ray diffraction
3.2Å resolution

Core (C) protein from West Nile Virus, subtype Kunjin

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:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-146906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein C Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 76 amino acids
Theoretical weight: 8.62 KDa
Source organism: Kunjin virus (STRAIN MRM61C)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14335 (Residues: 23-98; Coverage: 2%)
Sequence domains: Flavivirus capsid protein C
Structure domains: Arc Repressor Mutant, subunit A

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I41
Unit cell:
a: 85.655Å b: 85.655Å c: 214.384Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.249 0.311
Expression system: Escherichia coli BL21(DE3)