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1lox
From Proteopedia
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|PDB= 1lox |SIZE=350|CAPTION= <scene name='initialview01'>1lox</scene>, resolution 2.4Å | |PDB= 1lox |SIZE=350|CAPTION= <scene name='initialview01'>1lox</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene> | |SITE= <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=RS7:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC+ACID'>RS7</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Arachidonate_15-lipoxygenase Arachidonate 15-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.33 1.13.11.33] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arachidonate_15-lipoxygenase Arachidonate 15-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.33 1.13.11.33] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lox OCA], [http://www.ebi.ac.uk/pdbsum/1lox PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lox RCSB]</span> | ||
}} | }} | ||
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[[Category: Sigal, E.]] | [[Category: Sigal, E.]] | ||
[[Category: Villasenor, A.]] | [[Category: Villasenor, A.]] | ||
| - | [[Category: FE2]] | ||
| - | [[Category: RS7]] | ||
[[Category: 15lo_depot2]] | [[Category: 15lo_depot2]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 22:05:29 2008'' |
Revision as of 19:05, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Arachidonate 15-lipoxygenase, with EC number 1.13.11.33 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RABBIT RETICULOCYTE 15-LIPOXYGENASE
Overview
Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.
About this Structure
1LOX is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550
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