› 2x3h

X-ray diffraction
1.6Å 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-126724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mature tail spike protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 542 amino acids
Theoretical weight: 56.38 KDa
Source organism: Escherichia virus K1-5
Expression system: Escherichia coli
UniProt:
  • Canonical: O09496 (Residues: 1-505; Coverage: 80%)
Gene name: kflA
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

1 bound ligand:
Ligand BR 12 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 68.53Å b: 130.4Å c: 145.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.203
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structural and mechanistic classification of uronic acid-containing polysaccharide lyases.
Garron et al. (2010)
10 more

5 mentions without citation

The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.
Thompson et al. (2010)
4 more