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==SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTION==
==SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTION==
<StructureSection load='1g0z' size='340' side='right' caption='[[1g0z]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
<StructureSection load='1g0z' size='340' side='right'caption='[[1g0z]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g0z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_caeruleus Bungarus caeruleus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g0z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_caeruleus Bungarus caeruleus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0Z FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fe5|1fe5]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0z OCA], [https://pdbe.org/1g0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0z RCSB], [https://www.ebi.ac.uk/pdbsum/1g0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0z ProSAT]</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=1g0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0z OCA], [http://pdbe.org/1g0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0z RCSB], [http://www.ebi.ac.uk/pdbsum/1g0z PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA2B5_BUNCE PA2B5_BUNCE] Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities.  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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0z_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0z_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Phospholipase A2|Phospholipase A2]]
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bungarus caeruleus]]
[[Category: Bungarus caeruleus]]
[[Category: Gourinath, S]]
[[Category: Large Structures]]
[[Category: Sharma, S]]
[[Category: Gourinath S]]
[[Category: Singh, G]]
[[Category: Sharma S]]
[[Category: Singh, T P]]
[[Category: Singh G]]
[[Category: Homodimer]]
[[Category: Singh TP]]
[[Category: Phospholipase a2]]
[[Category: Structure]]
[[Category: Toxin]]

Latest revision as of 02:59, 21 November 2024

SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTIONSPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTION

Structural highlights

1g0z is a 2 chain structure with sequence from Bungarus caeruleus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.18Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2B5_BUNCE Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1g0z, resolution 2.18Å

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