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2zbh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zbh]] is a 1 chain structure with sequence from [http://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=2ZBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZBH FirstGlance]. <br> | <table><tr><td colspan='2'>[[2zbh]] is a 1 chain structure with sequence from [http://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=2ZBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZBH FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BVL:(2E)-1-[2-HYDROXY-4-METHOXY-5-(3-METHYLBUT-2-EN-1-YL)PHENYL]-3-(4-HYDROXYPHENYL)PROP-2-EN-1-ONE'>BVL</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BVL:(2E)-1-[2-HYDROXY-4-METHOXY-5-(3-METHYLBUT-2-EN-1-YL)PHENYL]-3-(4-HYDROXYPHENYL)PROP-2-EN-1-ONE'>BVL</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qvd|2qvd]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qvd|2qvd]]</td></tr> |
| - | <tr><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> | + | <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> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zbh RCSB], [http://www.ebi.ac.uk/pdbsum/2zbh PDBsum]</span></td></tr> | + | <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=2zbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zbh RCSB], [http://www.ebi.ac.uk/pdbsum/2zbh PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PA28_DABRP PA28_DABRP]] 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:8835338</ref> <ref>PMID:2115497</ref> <ref>PMID:18062812</ref> | ||
== 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|Phospholipase A2]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Daboia russellii pulchella]] | [[Category: Daboia russellii pulchella]] | ||
| - | [[Category: Damodar, N C | + | [[Category: Damodar, N C]] |
| - | [[Category: Haridas, M | + | [[Category: Haridas, M]] |
| - | [[Category: Jain, R | + | [[Category: Jain, R]] |
| - | [[Category: Kaur, P | + | [[Category: Kaur, P]] |
| - | [[Category: Kumar, S | + | [[Category: Kumar, S]] |
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] |
| - | [[Category: Singh, N | + | [[Category: Singh, N]] |
| - | [[Category: Singh, T P | + | [[Category: Singh, T P]] |
| - | [[Category: Srinivasan, A | + | [[Category: Srinivasan, A]] |
[[Category: Aerva lanata]] | [[Category: Aerva lanata]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
Revision as of 03:35, 25 December 2014
Crystal structure of the complex of phospholipase A2 with Bavachalcone from Aerva lanata at 2.6 A resolution
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Categories: Daboia russellii pulchella | Damodar, N C | Haridas, M | Jain, R | Kaur, P | Kumar, S | Sharma, S | Singh, N | Singh, T P | Srinivasan, A | Aerva lanata | Complex | Daucosterol | Hydrolase | Lipid degradation | Metal-binding | Neurotoxin | Phospholipse a2 | Presynaptic neurotoxin | Secreted | Toxin

