2que
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2que' size='340' side='right'caption='[[2que]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2que' size='340' side='right'caption='[[2que]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2que]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2que]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_pulchella Daboia russellii pulchella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QUE FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJM:AJMALINE'>AJM</scene>, <scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJM:AJMALINE'>AJM</scene>, <scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pyc|2pyc]], [[2oub|2oub]], [[2oth|2oth]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pyc|2pyc]], [[2oub|2oub]], [[2oth|2oth]]</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=2que FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2que OCA], [https://pdbe.org/2que PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2que RCSB], [https://www.ebi.ac.uk/pdbsum/2que PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2que ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PA2B8_DABRR PA2B8_DABRR]] Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18062812</ref> <ref>PMID:2115497</ref> <ref>PMID:8835338</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:45, 16 March 2022
Saturation of substrate-binding site using two natural ligands: Crystal structure of a ternary complex of phospholipase A2 with anisic acid and ajmaline at 2.25 A resolution
| |||||||||||
