› 3ah2

X-ray diffraction
1.7Å resolution

HA1 subcomponent of botulinum type C progenitor toxin complexed with N-acetylgalactosamine

Released:
DOI: 10.2210/pdb3ah2/pdb
PDB entry 3ah2 coloured by chain, front view.
PDB entry 3ah2 coloured by chain, side view.
PDB entry 3ah2 coloured by chain, top view.
Source organism: Clostridium botulinum
Primary publication:
Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin.
Nakamura T, Tonozuka T, Ide A, Yuzawa T, Oguma K, Nishikawa A
J Mol Biol 376 854-67 (2008)
PMID: 18178224

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-144104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Main hemagglutinin component type C Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 34.08 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DPR0 (Residues: 1-286; Coverage: 100%)
Gene names: HA-33, antP-33, ha1
Sequence domains: Ricin-type beta-trefoil lectin domain-like
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
Ligand NGA 1 x NGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 137.937Å b: 62.061Å c: 82.426Å
α: 90° β: 104.22° γ: 90°
R-values:
R R work R free
0.177 0.174 0.203
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology.
Pirazzini et al. (2017)
6 more

3 mentions without citation

Dicarbonyl stress, protein glycation and the unfolded protein response.
Rabbani et al. (2021)
2 more