1bci

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==C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE==
==C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE==
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<StructureSection load='1bci' size='340' side='right' caption='[[1bci]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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<StructureSection load='1bci' size='340' side='right'caption='[[1bci]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1bci]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1bci]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BCI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bci OCA], [http://pdbe.org/1bci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bci RCSB], [http://www.ebi.ac.uk/pdbsum/1bci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bci ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bci OCA], [https://pdbe.org/1bci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bci RCSB], [https://www.ebi.ac.uk/pdbsum/1bci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bci ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PA24A_HUMAN PA24A_HUMAN]] Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
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[https://www.uniprot.org/uniprot/PA24A_HUMAN PA24A_HUMAN] Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bci_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bci_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 1bci" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1bci" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Clark, J D]]
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[[Category: Large Structures]]
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[[Category: Cumming, D A]]
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[[Category: Clark JD]]
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[[Category: Mcdonagh, T]]
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[[Category: Cumming DA]]
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[[Category: Nalefski, E A]]
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[[Category: Mcdonagh T]]
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[[Category: Xu, G Y]]
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[[Category: Nalefski EA]]
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[[Category: Yu, H A]]
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[[Category: Xu GY]]
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[[Category: C2 domain]]
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[[Category: Yu HA]]
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[[Category: Calcium-dependent lipid binding]]
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[[Category: Cytosolic phospholipase a2]]
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[[Category: Hydrolase]]
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[[Category: Lipid degradation]]
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[[Category: Phosphocholine]]
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Current revision

C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE

PDB ID 1bci

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