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1ae7
From Proteopedia
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|PDB= 1ae7 |SIZE=350|CAPTION= <scene name='initialview01'>1ae7</scene>, resolution 2.0Å | |PDB= 1ae7 |SIZE=350|CAPTION= <scene name='initialview01'>1ae7</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=CAL:Site+*Cal*+Comprises+Those+Residues+Forming+The+Ca2++Bin+...'>CAL</scene> and <scene name='pdbsite=CNR:Site+*Cnr*+Comprises+Those+Residues+Forming+The+Catalyti+...'>CNR</scene> | |SITE= <scene name='pdbsite=CAL:Site+*Cal*+Comprises+Those+Residues+Forming+The+Ca2++Bin+...'>CAL</scene> and <scene name='pdbsite=CNR:Site+*Cnr*+Comprises+Those+Residues+Forming+The+Catalyti+...'>CNR</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ae7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ae7 OCA], [http://www.ebi.ac.uk/pdbsum/1ae7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ae7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Uhlin, U.]] | [[Category: Uhlin, U.]] | ||
[[Category: Westerlund, B.]] | [[Category: Westerlund, B.]] | ||
| - | [[Category: SO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: lipid degradation]] | [[Category: lipid degradation]] | ||
| Line 35: | Line 37: | ||
[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:38:20 2008'' |
Revision as of 15:38, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NOTEXIN, A PRESYNAPTIC NEUROTOXIC PHOSPHOLIPASE A2
Overview
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.
About this Structure
1AE7 is a Single protein structure of sequence from Notechis scutatus scutatus. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at 2.0 A resolution., Westerlund B, Nordlund P, Uhlin U, Eaker D, Eklund H, FEBS Lett. 1992 Apr 20;301(2):159-64. PMID:1568473
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