PDBe 1v0f

X-ray diffraction
2.55Å resolution

ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tail spike protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 666 amino acids
Theoretical weight: 74.13 KDa
Source organism: Enterobacteria phage K1F
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04830 (Residues: 245-910; Coverage: 63%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P2221
Unit cell:
a: 99.54Å b: 131.4Å c: 346.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.232
Expression system: Escherichia coli