1p2d - Revision history

OCA at 07:22, 25 October 2023

OCA — Wed, 25 Oct 2023 07:22:05 GMT

←Older revision		Revision as of 07:22, 25 October 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GLC:ALPHA~~-~~D-GLUCOSE'>GLC</scene>~~, ~~<scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.94Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1]~~ </~~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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [https://pdbe.org/1p2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [https://www.ebi.ac.uk/pdbsum/1p2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2d 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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [https://pdbe.org/1p2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [https://www.ebi.ac.uk/pdbsum/1p2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.	+	[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	~~[[Category: Phosphorylase]]~~	+	[[Category: Chrysina ED]]
-	[[Category: Chrysina~~, E D~~]]	+	[[Category: Leonidas DD]]
-	[[Category: Leonidas~~, D D~~]]	+	[[Category: Mavridis IM]]
-	[[Category: Mavridis~~, I M~~]]	+	[[Category: Oikonomakos NG]]
-	[[Category: Oikonomakos~~, N G~~]]	+	[[Category: Pinotsis N]]
-	[[Category: Pinotsis, N]]	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:58, 21 April 2021

OCA — Wed, 21 Apr 2021 08:58:40 GMT

←Older revision		Revision as of 08:58, 21 April 2021
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	<StructureSection load='1p2d' size='340' side='right'caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='1p2d' size='340' side='right'caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~European_rabbit European rabbit~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1P2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [~~http~~://pdbe.org/1p2d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1p2d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2d 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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [https://pdbe.org/1p2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [https://www.ebi.ac.uk/pdbsum/1p2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.	+	[[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	== 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>
-	[[Category: European rabbit]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Chrysina, E D]]		[[Category: Chrysina, E D]]

OCA at 13:39, 17 July 2019

OCA — Wed, 17 Jul 2019 13:39:37 GMT

←Older revision		Revision as of 13:39, 17 July 2019
Line 1:		Line 1:

	==Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin==		==Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin==
-	<StructureSection load='1p2d' size='340' side='right' caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>	+	<StructureSection load='1p2d' size='340' side='right'caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p2/1p2d_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p2/1p2d_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1p2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p2d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: European rabbit]]		[[Category: European rabbit]]
		+	[[Category: Large Structures]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Chrysina, E D]]		[[Category: Chrysina, E D]]

OCA at 14:29, 12 October 2017

OCA — Thu, 12 Oct 2017 14:29:31 GMT

←Older revision		Revision as of 14:29, 12 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin==		==Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin==
	<StructureSection load='1p2d' size='340' side='right' caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='1p2d' size='340' side='right' caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Oryctolagus_cuniculus Oryctolagus cuniculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://pdbe.org/1p2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d 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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://pdbe.org/1p2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=1p2d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1p2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p2d" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Oryctolagus cuniculus~~]]	+	[[Category: European rabbit]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Chrysina, E D]]		[[Category: Chrysina, E D]]

OCA at 01:53, 12 September 2015

OCA — Sat, 12 Sep 2015 01:53:50 GMT

←Older revision		Revision as of 01:53, 12 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d 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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://pdbe.org/1p2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1p2d" style="background-color:#fffaf0;"></div>

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

OCA at 22:17, 25 December 2014

OCA — Thu, 25 Dec 2014 22:17:55 GMT

←Older revision		Revision as of 22:17, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d 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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
-	[[Category: Chrysina, E D.]]	+	[[Category: Chrysina, E D]]
-	[[Category: Leonidas, D D.]]	+	[[Category: Leonidas, D D]]
-	[[Category: Mavridis, I M.]]	+	[[Category: Mavridis, I M]]
-	[[Category: Oikonomakos, N G.]]	+	[[Category: Oikonomakos, N G]]
-	[[Category: Pinotsis, N.]]	+	[[Category: Pinotsis, N]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 23:36, 28 September 2014

OCA — Sun, 28 Sep 2014 23:36:42 GMT

←Older revision		Revision as of 23:36, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1p2d.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin==
		+	<StructureSection load='1p2d' size='340' side='right' caption='[[1p2d]], [[Resolution\|resolution]] 1.94Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P2D FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p29\|1p29]], [[1p2b\|1p2b]], [[1p2g\|1p2g]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=1p2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p2d RCSB], [http://www.ebi.ac.uk/pdbsum/1p2d 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/p2/1p2d_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 ==
		+	A number of regulatory binding sites of glycogen phosphorylase (GP), such as the catalytic, the inhibitor, and the new allosteric sites are currently under investigation as targets for inhibition of hepatic glycogenolysis under high glucose concentrations; in some cases specific inhibitors are under evaluation in human clinical trials for therapeutic intervention in type 2 diabetes. In an attempt to investigate whether the storage site can be exploited as target for modulating hepatic glucose production, alpha-, beta-, and gamma-cyclodextrins were identified as moderate mixed-type competitive inhibitors of GPb (with respect to glycogen) with K(i) values of 47.1, 14.1, and 7.4 mM, respectively. To elucidate the structural basis of inhibition, we determined the structure of GPb complexed with beta- and gamma-cyclodextrins at 1.94 A and 2.3 A resolution, respectively. The structures of the two complexes reveal that the inhibitors can be accommodated in the glycogen storage site of T-state GPb with very little change of the tertiary structure and provide a basis for understanding their potency and subsite specificity. Structural comparisons of the two complexes with GPb in complex with either maltopentaose (G5) or maltoheptaose (G7) show that beta- and gamma-cyclodextrins bind in a mode analogous to the G5 and G7 binding with only some differences imposed by their cyclic conformations. It appears that the binding energy for stabilization of enzyme complexes derives from hydrogen bonding and van der Waals contacts to protein residues. The binding of alpha-cyclodextrin and octakis (2,3,6-tri-O-methyl)-gamma-cyclodextrin was also investigated, but none of them was bound in the crystal; moreover, the latter did not inhibit the phosphorylase reaction.

-	~~{{STRUCTURE_1p2d\| PDB=1p2d \| SCENE= }}~~	+	The binding of beta- and gamma-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies.,Pinotsis N, Leonidas DD, Chrysina ED, Oikonomakos NG, Mavridis IM Protein Sci. 2003 Sep;12(9):1914-24. PMID:12930991<ref>PMID:12930991</ref>

-	~~===Crystal Structure~~ of ~~Glycogen Phosphorylase B in complex with Beta Cyclodextrin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12930991}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1p2d]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA].~~	+

	==See Also==		==See Also==
	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]		*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012930991<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 22:18, 20 October 2012

OCA — Sat, 20 Oct 2012 22:18:40 GMT

←Older revision		Revision as of 22:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1p2d]] is a 1 chain structure ~~of [[Glycogen Phosphorylase]]~~ with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA].	+	[[1p2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA].

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

OCA: Protected "1p2d" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 15:53:21 GMT

Protected "1p2d" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:53, 27 July 2012

OCA at 15:53, 27 July 2012

OCA — Fri, 27 Jul 2012 15:53:19 GMT

←Older revision		Revision as of 15:53, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1p2d.png\|left\|200px]]		[[Image:1p2d.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1p2d", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1p2d\| PDB=1p2d \| SCENE= }}		{{STRUCTURE_1p2d\| PDB=1p2d \| SCENE= }}

	===Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin===		===Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12930991}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12930991 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12930991}}		{{ABSTRACT_PUBMED_12930991}}

	==About this Structure==		==About this Structure==
-	~~1P2D~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA].	+	[[1p2d]] is a 1 chain structure of [[Glycogen Phosphorylase]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2D OCA].
		+
		+	==See Also==
		+	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12930991~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012930991</ref><references group="xtra"/>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
Line 32:		Line 23:
	[[Category: Pinotsis, N.]]		[[Category: Pinotsis, N.]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:33:36 2009''