4h5m

X-ray diffraction
3.1Å resolution

Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Hexamer

Released:
Source organism: Rift Valley fever virus
Primary publication:
Phleboviruses encapsidate their genomes by sequestering RNA bases.
Proc Natl Acad Sci U S A 109 19208-13 (2012)
PMID: 23129612

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoprotein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 245 amino acids
Theoretical weight: 27.37 KDa
Source organism: Rift Valley fever virus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D3K5I7 (Residues: 1-245; Coverage: 100%)
Gene name: N
Sequence domains: Tenuivirus/Phlebovirus nucleocapsid protein

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3121
Unit cell:
a: 107.13Å b: 107.13Å c: 258.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.256
Expression system: Escherichia coli BL21