1dpy - Revision history

OCA at 09:52, 20 March 2024

2024-03-20T09:52:36Z

←Older revision		Revision as of 09:52, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPY FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.45Å</td></tr>
-	<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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [https://pdbe.org/1dpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [https://www.ebi.ac.uk/pdbsum/1dpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpy 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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [https://pdbe.org/1dpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [https://www.ebi.ac.uk/pdbsum/1dpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpy ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PA2B_BUNCE PA2B_BUNCE]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpy ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	This is the first phospholipase A2 (PLA2) structure from the family of kraits. The protein was isolated from Bungarus caeruleus (common krait) and the primary sequence was determined using cDNA approach. Three-dimensional structure of this presynaptic neurotoxic PLA2 from group I has been determined by molecular replacement method using the model of PLA2 component of beta2-bungarotoxin (Bungarus multicinctus) and refined using CNS package to a final R-factor of 20.1 % for all the data in resolution range 20.0-2.4 A. The final refined model comprises 897 protein atoms and 77 water molecules. The overall framework of krait phospholipase A2 with three long helices and two short antiparallel beta-strands is extremely similar to those observed for other group I PLA2s. However, the critical parts of PLA2 folding are concerned with its various functional loops. The conformations of these loops determine the efficiency of enzyme action and presence/absence of various pharmacological functions. In the present structure calcium-binding loop is occupied by a sodium ion with a 7-fold co-ordination. The conformation of loop 55-75 in krait PLA2 corresponds to a very high activity of the enzyme. A comparison of its sequence with multimeric PLA2s clearly shows the absence of critical residues such as Tyr3, Trp61 and Phe64, which are involved in the multimerization of PLA2 molecules. The protein shows anticoagulant and neurotoxic activities.
-
-	Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.,Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP J Mol Biol. 2001 Apr 6;307(4):1049-59. PMID:11286555<ref>PMID:11286555</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dpy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Phospholipase A2 3D structures\|Phospholipase A2 3D structures]]		*[[Phospholipase A2 3D structures\|Phospholipase A2 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bungarus caeruleus]]		[[Category: Bungarus caeruleus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gourinath, S]]	+	[[Category: Gourinath S]]
-	[[Category: Paramasivam, M]]	+	[[Category: Paramasivam M]]
-	[[Category: Sharma, S]]	+	[[Category: Sharma S]]
-	[[Category: Singh, G]]	+	[[Category: Singh G]]
-	[[Category: Singh~~, T P~~]]	+	[[Category: Singh TP]]
-	[[Category: Srinivasan, A]]	+	[[Category: Srinivasan A]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Indian common krait venom]]~~	+
-	~~[[Category: Phospholipase a2]]~~	+
-	~~[[Category: Refinement~~]]	+

OCA at 18:32, 10 March 2021

2021-03-10T18:32:33Z

←Older revision		Revision as of 18:32, 10 March 2021
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	<StructureSection load='1dpy' size='340' side='right'caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>		<StructureSection load='1dpy' size='340' side='right'caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DPY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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='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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [~~http~~://pdbe.org/1dpy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dpy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpy 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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [https://pdbe.org/1dpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [https://www.ebi.ac.uk/pdbsum/1dpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpy ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 29:		Line 29:

	==See Also==		==See Also==
-	*[[Phospholipase A2\|Phospholipase A2]]	+	*[[Phospholipase A2 3D structures\|Phospholipase A2 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 23:27, 5 June 2019

2019-06-05T23:27:31Z

←Older revision		Revision as of 23:27, 5 June 2019
Line 1:		Line 1:

	==THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION==		==THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION==
-	<StructureSection load='1dpy' size='340' side='right' caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>	+	<StructureSection load='1dpy' size='340' side='right'caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DPY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DPY FirstGlance]. <br>
Line 12:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpy_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Bungarus caeruleus]]		[[Category: Bungarus caeruleus]]
		+	[[Category: Large Structures]]
	[[Category: Gourinath, S]]		[[Category: Gourinath, S]]
	[[Category: Paramasivam, M]]		[[Category: Paramasivam, M]]

OCA at 04:03, 30 August 2017

2017-08-30T04:03:33Z

←Older revision		Revision as of 04:03, 30 August 2017
Line 1:		Line 1:
		+
	==THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION==		==THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION==
	<StructureSection load='1dpy' size='340' side='right' caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>		<StructureSection load='1dpy' size='340' side='right' caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://pdbe.org/1dpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy 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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://pdbe.org/1dpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpy ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:30, 11 September 2015

2015-09-11T13:30:33Z

←Older revision		Revision as of 13:30, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy 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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://pdbe.org/1dpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1dpy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 21:46, 22 December 2014

2014-12-22T21:46:50Z

←Older revision		Revision as of 21:46, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DPY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DPY FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy 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=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Bungarus caeruleus]]		[[Category: Bungarus caeruleus]]
-	[[Category: Gourinath, S.]]	+	[[Category: Gourinath, S]]
-	[[Category: Paramasivam, M.]]	+	[[Category: Paramasivam, M]]
-	[[Category: Sharma, S.]]	+	[[Category: Sharma, S]]
-	[[Category: Singh, G.]]	+	[[Category: Singh, G]]
-	[[Category: Singh, T P.]]	+	[[Category: Singh, T P]]
-	[[Category: Srinivasan, A.]]	+	[[Category: Srinivasan, A]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Indian common krait venom]]		[[Category: Indian common krait venom]]
	[[Category: Phospholipase a2]]		[[Category: Phospholipase a2]]
	[[Category: Refinement]]		[[Category: Refinement]]

OCA at 10:37, 10 September 2014

2014-09-10T10:37:29Z

←Older revision		Revision as of 10:37, 10 September 2014
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-	[[~~Image~~:1dpy.~~png\|left~~\|200px]]	+	==THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION==
		+	<StructureSection load='1dpy' size='340' side='right' caption='[[1dpy]], [[Resolution\|resolution]] 2.45Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dpy]] is a 1 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=1DPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DPY FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpy RCSB], [http://www.ebi.ac.uk/pdbsum/1dpy PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpy_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	This is the first phospholipase A2 (PLA2) structure from the family of kraits. The protein was isolated from Bungarus caeruleus (common krait) and the primary sequence was determined using cDNA approach. Three-dimensional structure of this presynaptic neurotoxic PLA2 from group I has been determined by molecular replacement method using the model of PLA2 component of beta2-bungarotoxin (Bungarus multicinctus) and refined using CNS package to a final R-factor of 20.1 % for all the data in resolution range 20.0-2.4 A. The final refined model comprises 897 protein atoms and 77 water molecules. The overall framework of krait phospholipase A2 with three long helices and two short antiparallel beta-strands is extremely similar to those observed for other group I PLA2s. However, the critical parts of PLA2 folding are concerned with its various functional loops. The conformations of these loops determine the efficiency of enzyme action and presence/absence of various pharmacological functions. In the present structure calcium-binding loop is occupied by a sodium ion with a 7-fold co-ordination. The conformation of loop 55-75 in krait PLA2 corresponds to a very high activity of the enzyme. A comparison of its sequence with multimeric PLA2s clearly shows the absence of critical residues such as Tyr3, Trp61 and Phe64, which are involved in the multimerization of PLA2 molecules. The protein shows anticoagulant and neurotoxic activities.

-	~~{{STRUCTURE_1dpy\| PDB=1dpy \| SCENE= }}~~	+	Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.,Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP J Mol Biol. 2001 Apr 6;307(4):1049-59. PMID:11286555<ref>PMID:11286555</ref>

-	~~===THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11286555}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1dpy]] is~~ a ~~1 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=1DPY OCA].~~	+

	==See Also==		==See Also==
	*[[Phospholipase A2\|Phospholipase A2]]		*[[Phospholipase A2\|Phospholipase A2]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011286555<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bungarus caeruleus]]		[[Category: Bungarus caeruleus]]
	[[Category: Gourinath, S.]]		[[Category: Gourinath, S.]]

OCA at 19:15, 20 October 2012

2012-10-20T19:15:20Z

←Older revision		Revision as of 19:15, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[1dpy]] is a 1 chain structure ~~of [[Phospholipase A2]]~~ 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=1DPY OCA].	+	[[1dpy]] is a 1 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=1DPY OCA].

	==See Also==		==See Also==

OCA at 06:45, 27 July 2012

2012-07-27T06:45:30Z

←Older revision		Revision as of 06:45, 27 July 2012
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	[[Image:1dpy.png\|left\|200px]]		[[Image:1dpy.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1dpy\| PDB=1dpy \| SCENE= }}		{{STRUCTURE_1dpy\| PDB=1dpy \| SCENE= }}

	===THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION===		===THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION===

-
-	<!--
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-	(as it appears on PubMed at http://www.pubmed.gov), where 11286555 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_11286555}}		{{ABSTRACT_PUBMED_11286555}}

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	==See Also==		==See Also==
-	*[[Phospholipase A2]]	+	*[[Phospholipase A2\|Phospholipase A2]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11286555~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011286555</ref><references group="xtra"/>
	[[Category: Bungarus caeruleus]]		[[Category: Bungarus caeruleus]]
	[[Category: Gourinath, S.]]		[[Category: Gourinath, S.]]
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	[[Category: Singh, T P.]]		[[Category: Singh, T P.]]
	[[Category: Srinivasan, A.]]		[[Category: Srinivasan, A.]]
-	[[Category: Crystal structure]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Indian common krait venom]]		[[Category: Indian common krait venom]]
	[[Category: Phospholipase a2]]		[[Category: Phospholipase a2]]
	[[Category: Refinement]]		[[Category: Refinement]]

OCA: Protected "1dpy" [edit=sysop:move=sysop]

2010-12-26T23:34:57Z

Protected "1dpy" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:34, 26 December 2010