1sqz

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<StructureSection load='1sqz' size='340' side='right'caption='[[1sqz]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='1sqz' size='340' side='right'caption='[[1sqz]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1sqz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_russellii Daboia russellii russellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1sqz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russelii_russelii Daboia russelii russelii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></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=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fb2|1fb2]]</div></td></tr>
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<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>
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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=1sqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqz OCA], [https://pdbe.org/1sqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqz RCSB], [https://www.ebi.ac.uk/pdbsum/1sqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqz ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqz OCA], [https://pdbe.org/1sqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqz RCSB], [https://www.ebi.ac.uk/pdbsum/1sqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Daboia russellii russellii]]
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[[Category: Daboia russelii russelii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bilgrami, S]]
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[[Category: Bilgrami S]]
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[[Category: Dey, S]]
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[[Category: Dey S]]
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[[Category: Ethayathulla, A S]]
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[[Category: Ethayathulla AS]]
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[[Category: Kumar, R Prem]]
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[[Category: Prem Kumar R]]
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[[Category: Sharma, S]]
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[[Category: Sharma S]]
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[[Category: Singh, N]]
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[[Category: Singh N]]
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[[Category: Singh, T P]]
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[[Category: Singh TP]]
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[[Category: Somvanshi, R K]]
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[[Category: Somvanshi RK]]
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[[Category: Dehydro-iar]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Phospholipase a2]]
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[[Category: Toxin]]
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Revision as of 06:20, 23 August 2023

Design of specific inhibitors of Phopholipase A2: Crystal structure of the complex formed between Group II Phopholipase A2 and a designed peptide Dehydro-Ile-Ala-Arg-Ser at 1.2A resolution

PDB ID 1sqz

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OCA

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