› 2vbe

X-ray diffraction
1.98Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tail spike protein Chain: A
Molecule details ›
Chain: A
Length: 514 amino acids
Theoretical weight: 55.31 KDa
Source organism: Shigella virus Sf6
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9XJP3 (Residues: 110-623; Coverage: 83%)
Sequence domains:
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

4 bound ligands:
Ligand MN 1 x MN
Ligand CA 2 x CA
Ligand EDO 6 x EDO
Ligand PO4 2 x PO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: R3
Unit cell:
a: 95.91Å b: 95.91Å c: 182.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.119 0.117 0.149
Expression system: Escherichia coli

Quick links

Citations

8 review citations

A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries.
Veesler et al. (2011)
7 more

3 mentions without citation

Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.
Ishida et al. (2009)
2 more