1jlt: Difference between revisions
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<StructureSection load='1jlt' size='340' side='right'caption='[[1jlt]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1jlt' size='340' side='right'caption='[[1jlt]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jlt]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jlt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vipera_ammodytes_ammodytes Vipera ammodytes ammodytes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JLT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aok|1aok]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aok|1aok]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlt OCA], [https://pdbe.org/1jlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jlt RCSB], [https://www.ebi.ac.uk/pdbsum/1jlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jlt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PA2A_VIPAE PA2A_VIPAE]] Heterodimer: postsynaptic neurotoxin.<ref>PMID:23554559</ref> Monomer: Acidic phospholipase A2 homolog that is non-toxic.<ref>PMID:23554559</ref> [[https://www.uniprot.org/uniprot/PA2B_VIPAE PA2B_VIPAE]] Heterodimer: postsynaptic neurotoxin. Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Phospholipase A2|Phospholipase A2]] | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||