› 2vbk

X-ray diffraction
1.25Å 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: 55.03 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

6 bound ligands:
Ligand MG 2 x MG
Ligand EDO 12 x EDO
Ligand PGR 2 x PGR
Ligand GOL 6 x GOL
Ligand PO4 3 x PO4
Ligand CO2 2 x CO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: R3
Unit cell:
a: 96.231Å b: 96.231Å c: 182.433Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.12 0.119 0.142
Expression system: Escherichia coli

Quick links

Citations

9 review citations

A new era for understanding amyloid structures and disease.
Iadanza et al. (2018)
8 more

3 mentions without citation

Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures.
Parent et al. (2012)
2 more