› 1aho

X-ray diffraction
0.96Å resolution

THE AB INITIO STRUCTURE DETERMINATION AND REFINEMENT OF A SCORPION PROTEIN TOXIN

Released:
DOI: 10.2210/pdb1aho/pdb
PDB entry 1aho coloured by chain, front view.
PDB entry 1aho coloured by chain, side view.
PDB entry 1aho coloured by chain, top view.
Source organism: Androctonus australis hector
Primary publication:
Ab initio structure determination and refinement of a scorpion protein toxin.
Smith GD, Blessing RH, Ealick SE, Fontecilla-Camps JC, Hauptman HA, Housset D, Langs DA, Miller R
Acta Crystallogr D Biol Crystallogr 53 551-7 (1997)
PMID: 15299886

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-mammal toxin AaH2 Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.26 KDa
Source organism: Androctonus australis hector
UniProt:
  • Canonical: P01484 (Residues: 20-83; Coverage: 97%)
Sequence domains: Scorpion toxin-like domain
Structure domains: Knottin, scorpion toxin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 45.9Å b: 40.7Å c: 30.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 not available

Quick links

Citations

4 review citations

Advances in direct methods for protein crystallography.
Usón et al. (1999)
3 more

40 mentions without citation

Biomolecular Simulations with the Three-Dimensional Reference Interaction Site Model with the Kovalenko-Hirata Closure Molecular Solvation Theory.
Roy et al. (2021)
39 more