1AE7
NOTEXIN, A PRESYNAPTIC NEUROTOXIC PHOSPHOLIPASE A2
Summary for 1AE7
| Entry DOI | 10.2210/pdb1ae7/pdb |
| Descriptor | PHOSPHOLIPASE A2, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, phospholipase a2, lipid degradation, presynaptic neurotoxin, venom |
| Biological source | Notechis scutatus scutatus |
| Cellular location | Secreted: P00608 |
| Total number of polymer chains | 1 |
| Total formula weight | 13900.68 |
| Authors | Westerlund, B.,Nordlund, P.,Uhlin, U.,Eaker, D.,Eklund, H. (deposition date: 1997-03-06, release date: 1997-05-15, Last modification date: 2024-10-09) |
| Primary citation | Westerlund, B.,Nordlund, P.,Uhlin, U.,Eaker, D.,Eklund, H. The three-dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at 2.0 A resolution. FEBS Lett., 301:159-164, 1992 Cited by PubMed Abstract: The three-dimensional structure of notexin has been solved by molecular replacement methods. The structure has been refined at 2.0 A resolution to a crystallographic R-value of 16.5% with good stereo-chemistry. The core of the protein is very similar to other phospholipase A2s (PLA2 s) but several parts of the molecule are distinctly different. The most significant differences from PLA2 s from bovine pancreas and rattlesnake occur in the stretches 56-80 and 85-89. Residue 69, which has been shown to be important for phospholipase binding, has a different conformation and different interactions than in other known PLA2s. The C alpha positions for residues 86-88 differ by about 6 A from both the bovine and the rattlesnake enzyme. The crystals contain no Ca2+ ions. Instead, a water molecule occupies the calcium site. PubMed: 1568473DOI: 10.1016/0014-5793(92)81238-H PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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