PDBe 3gw6

X-ray diffraction
2.6Å resolution

Intramolecular Chaperone

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:
homo 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: 275 amino acids
Theoretical weight: 30.71 KDa
Source organism: Enterobacteria phage K1F
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04830 (Residues: 790-1064; Coverage: 26%)
Sequence domains: Chaperone of endosialidase
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P1
Unit cell:
a: 62.65Å b: 79.95Å c: 109.58Å
α: 81.71° β: 76.53° γ: 87.11°
R-values:
R R work R free
0.211 0.209 0.254
Expression system: Escherichia coli