› 2abx

X-ray diffraction
2.5Å resolution

THE CRYSTAL STRUCTURE OF ALPHA-BUNGAROTOXIN AT 2.5 ANGSTROMS RESOLUTION. RELATION TO SOLUTION STRUCTURE AND BINDING TO ACETYLCHOLINE RECEPTOR

Released:
DOI: 10.2210/pdb2abx/pdb
PDB entry 2abx coloured by chain, front view.
PDB entry 2abx coloured by chain, side view.
PDB entry 2abx coloured by chain, top view.
Source organism: Bungarus multicinctus
Primary publication:
The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor.
Love RA, Stroud RM
Protein Eng 1 37-46
PMID: 3507686

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-bungarotoxin Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 8.01 KDa
Source organism: Bungarus multicinctus
Expression system: Not provided
UniProt:
  • Canonical: P60615 (Residues: 22-95; Coverage: 100%)
Structure domains: CD59

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 67.8Å b: 78.4Å c: 22.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels.
Sixma et al. (2003)
8 more

7 mentions without citation

Snake Venom Peptides: Tools of Biodiscovery.
Munawar et al. (2018)
6 more