5bqu

X-ray diffraction
2.38Å resolution

Crystal structure of HA17-HA33-Lactulose

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-175079 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Ricin B lectin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 34.08 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45871 (Residues: 2-293; Coverage: 100%)
Gene names: HA, HA-33, ha33, ha34
Sequence domains: Ricin-type beta-trefoil lectin domain-like
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Hemagglutinin Chain: C
Molecule details ›
Chain: C
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45878 (Residues: 2-146; Coverage: 99%)
Gene names: EXM69_13435, HA, HA-17, ha17
Sequence domains: Clostridium botulinum HA-17 domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

Carbohydrate polymer : NEW Components: FRU, GAL
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2221
Unit cell:
a: 106.988Å b: 118.667Å c: 161.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.23
Expression system: Escherichia coli