› 3gvl

X-ray diffraction
1.41Å resolution

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids
Biochemical function:
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-170081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Mature tail spike protein Chain: A
Molecule details ›
Chain: A
Length: 670 amino acids
Theoretical weight: 74.54 KDa
Source organism: Escherichia phage K1F
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04830 (Residues: 246-910; Coverage: 63%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: SLB, SIA
Carbohydrate polymer
1 bound ligand:
Ligand SLB 1 x SLB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: R3
Unit cell:
a: 119.092Å b: 119.092Å c: 175.981Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.168 0.188
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration.
Schnaar et al. (2014)
7 more

1 mention without citation

The β-reducing end in α(2-8)-polysialic acid constitutes a unique structural motif.
Azurmendi et al. (2017)