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2sbl
From Proteopedia
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| - | [[Image:2sbl.jpg|left|200px]] | + | [[Image:2sbl.jpg|left|200px]] |
| - | + | ||
| - | '''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE''' | + | {{Structure |
| + | |PDB= 2sbl |SIZE=350|CAPTION= <scene name='initialview01'>2sbl</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SBL is a [ | + | 2SBL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SBL OCA]. |
==Reference== | ==Reference== | ||
| - | The three-dimensional structure of an arachidonic acid 15-lipoxygenase., Boyington JC, Gaffney BJ, Amzel LM, Science. 1993 Jun 4;260(5113):1482-6. PMID:[http:// | + | The three-dimensional structure of an arachidonic acid 15-lipoxygenase., Boyington JC, Gaffney BJ, Amzel LM, Science. 1993 Jun 4;260(5113):1482-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8502991 8502991] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Lipoxygenase]] | [[Category: Lipoxygenase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:12 2008'' |
Revision as of 16:38, 20 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Lipoxygenase, with EC number 1.13.11.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE
Overview
In mammals, the hydroperoxidation of arachidonic acid by lipoxygenases leads to the formation of leukotrienes and lipoxins, compounds that mediate inflammatory responses. Lipoxygenases are dioxygenases that contain a nonheme iron and are present in many animal cells. Soybean lipoxygenase-1 is a single-chain, 839-residue protein closely related to mammalian lipoxygenases. The structure of soybean lipoxygenase-1 solved to 2.6 angstrom resolution shows that the enzyme has two domains: a 146-residue beta barrel and a 693-residue helical bundle. The iron atom is in the center of the larger domain and is coordinated by three histidines and the COO- of the carboxyl terminus. The coordination geometry is nonregular and appears to be a distorted octahedron in which two adjacent positions are not occupied by ligands. Two cavities, in the shapes of a bent cylinder and a frustum, connect the unoccupied positions to the surface of the enzyme. The iron, with two adjacent and unoccupied positions, is poised to interact with the 1,4-diene system of the substrate and with molecular oxygen during catalysis.
About this Structure
2SBL is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of an arachidonic acid 15-lipoxygenase., Boyington JC, Gaffney BJ, Amzel LM, Science. 1993 Jun 4;260(5113):1482-6. PMID:8502991
Page seeded by OCA on Thu Mar 20 18:38:12 2008
