2gpn - Revision history

OCA at 06:44, 9 August 2023

OCA — Wed, 09 Aug 2023 06:44:39 GMT

←Older revision		Revision as of 06:44, 9 August 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=LLP:(2S)-2-AMINO-6~~-[[~~3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL~~]~~METHYLIDENEAMINO~~]~~HEXANOIC+ACID'>LLP</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]] 1.99Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [https://pdbe.org/2gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [https://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn 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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [https://pdbe.org/2gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [https://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn 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]]
Line 38:		Line 38:
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	[[Category: ~~Phosphorylase~~]]	+	[[Category: De La Fuente C]]
-	[[Category: Fleet~~, G W.J]]~~	+	[[Category: Fleet GWJ]]
-	~~[[Category: Fuente, C De La~~]]	+	[[Category: Garman EF]]
-	[[Category: Garman~~, E F~~]]	+	[[Category: Gregoriou M]]
-	[[Category: Gregoriou, M]]	+	[[Category: Johnson LN]]
-	[[Category: Johnson~~, L N~~]]	+	[[Category: Krulle TM]]
-	[[Category: Krulle~~, T M~~]]	+	[[Category: Noble MEM]]
-	[[Category: Noble~~, M E.M~~]]	+	[[Category: Oikonomakos NG]]
-	[[Category: Oikonomakos~~, N G~~]]	+	[[Category: Watson KA]]
-	[[Category: Watson~~, K A]]~~	+
-	~~[[Category: 100 k x-ray structure]]~~	+
-	~~[[Category: Glycogen phosphorylase]]~~	+
-	~~[[Category: Mpd]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Water structure~~]]	+

OCA at 14:46, 29 December 2021

OCA — Wed, 29 Dec 2021 14:46:54 GMT

←Older revision		Revision as of 14:46, 29 December 2021
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	<StructureSection load='2gpn' size='340' side='right'caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2gpn' size='340' side='right'caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2GPN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [~~http~~://pdbe.org/2gpn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn 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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [https://pdbe.org/2gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [https://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn 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]]

OCA at 11:17, 27 March 2020

OCA — Fri, 27 Mar 2020 11:17:53 GMT

←Older revision		Revision as of 11:17, 27 March 2020
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	==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION==		==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION==
-	<StructureSection load='2gpn' size='340' side='right' caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>	+	<StructureSection load='2gpn' size='340' side='right'caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Glycogen ~~Phosphorylase~~\|Glycogen ~~Phosphorylase~~]]	+	*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 07:01, 20 June 2018

OCA — Wed, 20 Jun 2018 07:01:16 GMT

←Older revision		Revision as of 07:01, 20 June 2018
Line 1:		Line 1:
		+
	==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION==		==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION==
	<StructureSection load='2gpn' size='340' side='right' caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2gpn' size='340' side='right' caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
-	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-~~LYSINE(~~3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-~~YLMETHANE)~~'>LLP</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://pdbe.org/2gpn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn 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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://pdbe.org/2gpn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/2gpn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/2gpn_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>
	</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=2gpn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:40, 12 September 2015

OCA — Sat, 12 Sep 2015 00:40:43 GMT

←Older revision		Revision as of 00:40, 12 September 2015
Line 5:		Line 5:
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn 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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://pdbe.org/2gpn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn 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 25:		Line 27:
	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 2gpn" style="background-color:#fffaf0;"></div>

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

OCA at 09:05, 16 January 2015

OCA — Fri, 16 Jan 2015 09:05:53 GMT

←Older revision		Revision as of 09:05, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn 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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
-	[[Category: Fleet, G W.J.]]	+	[[Category: Fleet, G W.J]]
-	[[Category: Fuente, C De La.]]	+	[[Category: Fuente, C De La]]
-	[[Category: Garman, E F.]]	+	[[Category: Garman, E F]]
-	[[Category: Gregoriou, M.]]	+	[[Category: Gregoriou, M]]
-	[[Category: Johnson, L N.]]	+	[[Category: Johnson, L N]]
-	[[Category: Krulle, T M.]]	+	[[Category: Krulle, T M]]
-	[[Category: Noble, M E.M.]]	+	[[Category: Noble, M E.M]]
-	[[Category: Oikonomakos, N G.]]	+	[[Category: Oikonomakos, N G]]
-	[[Category: Watson, K A.]]	+	[[Category: Watson, K A]]
	[[Category: 100 k x-ray structure]]		[[Category: 100 k x-ray structure]]
	[[Category: Glycogen phosphorylase]]		[[Category: Glycogen phosphorylase]]

OCA at 05:08, 29 September 2014

OCA — Mon, 29 Sep 2014 05:08:45 GMT

←Older revision		Revision as of 05:08, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:2gpn.~~png\|left~~\|200px]]	+	==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION==
		+	<StructureSection load='2gpn' size='340' side='right' caption='[[2gpn]], [[Resolution\|resolution]] 1.99Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GPN FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></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=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [http://www.ebi.ac.uk/pdbsum/2gpn 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/gp/2gpn_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 glucopyranose spirohydantoin (a pyranose analogue of the potent herbicide, hydantocidin) has been identified as the highest affinity glucose analogue inhibitor of glycogen phosphorylase b (GPb). In order to elucidate the structural features that contribute to the binding, the structures of GPb in the native T state conformation and in complex with glucopyranose spirohydantoin have been determined at 100 K to 2.0 A and 1.8 A resolution, respectively, and refined to crystallographic R values of 0.197 (R[free] 0.248) and 0.182 (R[free] 0.229), respectively. The low temperature structure of GPb is almost identical to that of the previously determined room temperature structure, apart from a decrease in overall atomic temperature factors ((B) room temperature GPb = 34.9 A2; (B) 100 K GPb = 23.4 A2). The glucopyranose spirohydantoin inhibitor (Ki = 3.0 microM) binds at the catalytic site and induces small changes in two key regions of the protein: the 280s loop (residues 281-286) that results in a decrease in mobility of this region, and the 380s loop (residues 377-385) that undergoes more significant shifts in order to optimize contact to the ligand. The hydantoin group, that is responsible for increasing the affinity of the glucose compound by a factor of 10(3), makes only one hydrogen bond to the protein, from one of its NH groups to the main chain oxygen of His377. The other polar groups of the hydantoin group form hydrogen bonds to five water molecules. These waters are involved in extensive networks of hydrogen bonds and appear to be an integral part of the protein structure. Analysis of the water structure at the catalytic site of the native enzyme, shows that five waters are displaced by ligand binding and that there is a significant decrease in mobility of the remaining waters on formation of the GPb-hydantoin complex. The ability of the inhibitor to exploit existing waters, to displace waters and to recruit new waters appears to be important for the high affinity of the inhibitor.

-	~~{{STRUCTURE_2gpn\| PDB=2gpn \| SCENE= }}~~	+	The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding.,Gregoriou M, Noble ME, Watson KA, Garman EF, Krulle TM, de la Fuente C, Fleet GW, Oikonomakos NG, Johnson LN Protein Sci. 1998 Apr;7(4):915-27. PMID:9568898<ref>PMID:9568898</ref>

-	~~===100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9568898}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2gpn]] 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=2GPN OCA].~~	+

	==See Also==		==See Also==
	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]		*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009568898<~~/~~ref~~><~~ref group="xtra">PMID:010548038</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 21:54, 20 October 2012

OCA — Sat, 20 Oct 2012 21:54:44 GMT

←Older revision		Revision as of 21:54, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2gpn]] 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=2GPN OCA].	+	[[2gpn]] 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=2GPN OCA].

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

OCA: Protected "2gpn" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 14:38:08 GMT

Protected "2gpn" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:38, 27 July 2012

OCA at 14:38, 27 July 2012

OCA — Fri, 27 Jul 2012 14:38:07 GMT

←Older revision		Revision as of 14:38, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2gpn.png\|left\|200px]]		[[Image:2gpn.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2gpn", 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.
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	{{STRUCTURE_2gpn\| PDB=2gpn \| SCENE= }}		{{STRUCTURE_2gpn\| PDB=2gpn \| SCENE= }}

	===100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION===		===100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9568898}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9568898 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9568898}}		{{ABSTRACT_PUBMED_9568898}}

	==About this Structure==		==About this Structure==
-	~~2GPN~~ 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=2GPN OCA].	+	[[2gpn]] 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=2GPN OCA].
		+
		+	==See Also==
		+	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9568898~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009568898</ref><ref group="xtra">PMID:010548038</ref><references group="xtra"/>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
Line 40:		Line 31:
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Water structure]]		[[Category: Water structure]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:25:15 2009''