1PTX
CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION
Summary for 1PTX
| Entry DOI | 10.2210/pdb1ptx/pdb |
| Descriptor | SCORPION TOXIN II (2 entities in total) |
| Functional Keywords | toxin |
| Biological source | Androctonus australis (Sahara scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 7262.17 |
| Authors | Fontecilla-Camps, J.C.,Housset, D. (deposition date: 1994-09-02, release date: 1995-01-26, Last modification date: 2024-10-16) |
| Primary citation | Housset, D.,Habersetzer-Rochat, C.,Astier, J.P.,Fontecilla-Camps, J.C. Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution. J.Mol.Biol., 238:88-103, 1994 Cited by PubMed Abstract: The crystal structure of toxin II from the scorpion Androctonus australis Hector has been refined at 1.3 A resolution using restrained least-squares methods. The final R-factor is 0.148 for the 13,619 reflections between 7.0 A and 1.3 A resolution with F > 2.5 sigma (F) and the bond length standard deviation from ideality is 0.017 A. Although minor changes have been introduced relative to the model previously refined at 1.8 A resolution, the use of higher-resolution data has allowed the modelling of some discrete disorder. Thus, three residues (including a disulphide bridge) have been built with multiple conformations. Occupancies were refined for the 106 solvent molecules included in the model, nine of them with explicit multiple sites. There is well-defined electron density for some of the protein hydrogen atoms in the final difference Fourier map. A detailed description of the toxin structure is presented, along with a comparison with the high-resolution structure of the related variant-3 scorpion toxin. PubMed: 8145259DOI: 10.1006/jmbi.1994.1270 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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