2c43 - Revision history

OCA at 14:04, 13 December 2023

2023-12-13T14:04:58Z

←Older revision		Revision as of 14:04, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2c43' size='340' side='right'caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>		<StructureSection load='2c43' size='340' side='right'caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C43 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.93Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2byd\|2byd]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </~~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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [https://pdbe.org/2c43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [https://www.ebi.ac.uk/pdbsum/2c43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c43 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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [https://pdbe.org/2c43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [https://www.ebi.ac.uk/pdbsum/2c43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c43 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN]] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>	+	[https://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: L-aminoadipate-semialdehyde dehydrogenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith, C]]	+	[[Category: Arrowsmith C]]
-	[[Category: Bunkoczi, G]]	+	[[Category: Bunkoczi G]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Dubinina E]]
-	[[Category: Dubinina, E]]	+	[[Category: Edwards A]]
-	[[Category: Edwards, A]]	+	[[Category: Johansson C]]
-	[[Category: Johansson, C]]	+	[[Category: Oppermann U]]
-	[[Category: Oppermann, U]]	+	[[Category: Smee C]]
-	[[Category: Smee, C]]	+	[[Category: Sundstrom M]]
-	[[Category: Sundstrom, M]]	+	[[Category: Turnbull A]]
-	[[Category: Turnbull, A]]	+	[[Category: Weigelt J]]
-	[[Category: Weigelt, J]]	+	[[Category: Wu X]]
-	[[Category: Wu, X]]	+	[[Category: Von Delft F]]
-	[[Category: ~~Coenzyme some]]~~	+
-	~~[[Category: Fatty acid biosynthesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 20:32, 20 October 2021

2021-10-20T20:32:43Z

←Older revision		Revision as of 20:32, 20 October 2021
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	<StructureSection load='2c43' size='340' side='right'caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>		<StructureSection load='2c43' size='340' side='right'caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2C43 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2byd\|2byd]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [~~http~~://pdbe.org/2c43 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2c43 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2c43 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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [https://pdbe.org/2c43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [https://www.ebi.ac.uk/pdbsum/2c43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c43 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN]] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>	+	[[https://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN]] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:04, 11 December 2019

2019-12-11T19:04:18Z

←Older revision		Revision as of 19:04, 11 December 2019
Line 1:		Line 1:

	==STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A==		==STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A==
-	<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>	+	<StructureSection load='2c43' size='340' side='right'caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
Line 36:		Line 36:
	[[Category: Human]]		[[Category: Human]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Arrowsmith, C]]		[[Category: Arrowsmith, C]]
	[[Category: Bunkoczi, G]]		[[Category: Bunkoczi, G]]

OCA at 18:46, 24 January 2018

2018-01-24T18:46:11Z

←Older revision		Revision as of 18:46, 24 January 2018
Line 1:		Line 1:
-	==STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A==	+
		+	==STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A==
	<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>		<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://pdbe.org/2c43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://pdbe.org/2c43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c43 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/2c43_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/2c43_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=2c43 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 37:		Line 38:
	[[Category: Arrowsmith, C]]		[[Category: Arrowsmith, C]]
	[[Category: Bunkoczi, G]]		[[Category: Bunkoczi, G]]
-	[[Category: Delft, F ~~Von~~]]	+	[[Category: Delft, F von]]
	[[Category: Dubinina, E]]		[[Category: Dubinina, E]]
	[[Category: Edwards, A]]		[[Category: Edwards, A]]

OCA at 09:40, 11 September 2015

2015-09-11T09:40:59Z

←Older revision		Revision as of 09:40, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>		<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://pdbe.org/2c43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 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 2c43" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
	[[Category: Arrowsmith, C]]		[[Category: Arrowsmith, C]]

OCA at 14:38, 25 December 2014

2014-12-25T14:38:32Z

←Older revision		Revision as of 14:38, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN]] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
-	[[Category: Arrowsmith, C.]]	+	[[Category: Arrowsmith, C]]
-	[[Category: Bunkoczi, G.]]	+	[[Category: Bunkoczi, G]]
-	[[Category: Delft, F Von.]]	+	[[Category: Delft, F Von]]
-	[[Category: Dubinina, E.]]	+	[[Category: Dubinina, E]]
-	[[Category: Edwards, A.]]	+	[[Category: Edwards, A]]
-	[[Category: Johansson, C.]]	+	[[Category: Johansson, C]]
-	[[Category: Oppermann, U.]]	+	[[Category: Oppermann, U]]
-	[[Category: Smee, C.]]	+	[[Category: Smee, C]]
-	[[Category: Sundstrom, M.]]	+	[[Category: Sundstrom, M]]
-	[[Category: Turnbull, A.]]	+	[[Category: Turnbull, A]]
-	[[Category: Weigelt, J.]]	+	[[Category: Weigelt, J]]
-	[[Category: Wu, X.]]	+	[[Category: Wu, X]]
	[[Category: Coenzyme some]]		[[Category: Coenzyme some]]
	[[Category: Fatty acid biosynthesis]]		[[Category: Fatty acid biosynthesis]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 02:20, 30 September 2014

2014-09-30T02:20:32Z

←Older revision		Revision as of 02:20, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2c43.~~png~~\|~~left~~\|200px]]	+	==STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A==
		+	<StructureSection load='2c43' size='340' side='right' caption='[[2c43]], [[Resolution\|resolution]] 1.93Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C43 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2byd\|2byd]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </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=2c43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c43 RCSB], [http://www.ebi.ac.uk/pdbsum/2c43 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/c4/2c43_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 ==
		+	Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed with CoA and Mg(2+), and in ternary complex with CoA and ACP. The involvement of key residues in ligand binding and catalysis was confirmed by mutagenesis and kinetic analysis. Human phosphopantetheinyl transferase exhibits an alpha/beta fold and 2-fold pseudosymmetry similar to the Sfp phosphopantetheinyl transferase from Bacillus subtilis. Although the bound ACP exhibits a typical four-helix structure, its binding is unusual in that it is facilitated predominantly by hydrophobic interactions. A detailed mechanism is proposed describing the substrate binding and catalytic process.

-	~~{{STRUCTURE_2c43\| PDB=2c43 \| SCENE= }}~~	+	Mechanism and substrate recognition of human holo ACP synthase.,Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U Chem Biol. 2007 Nov;14(11):1243-53. PMID:18022563<ref>PMID:18022563</ref>

-	~~===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18022563}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2c43]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:018022563<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]

OCA: Protected "2c43" [edit=sysop:move=sysop]

2013-01-06T11:33:13Z

Protected "2c43" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:33, 6 January 2013

OCA at 11:33, 6 January 2013

2013-01-06T11:33:10Z

←Older revision		Revision as of 11:33, 6 January 2013
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-	{{Seed}}
	[[Image:2c43.png\|left\|200px]]		[[Image:2c43.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2c43\| PDB=2c43 \| SCENE= }}		{{STRUCTURE_2c43\| PDB=2c43 \| SCENE= }}

	===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A===		===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18022563}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18022563 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18022563}}		{{ABSTRACT_PUBMED_18022563}}

	==About this Structure==		==About this Structure==
-	~~2C43~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA].	+	[[2c43]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18022563~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018022563</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
Line 40:		Line 28:
	[[Category: Coenzyme some]]		[[Category: Coenzyme some]]
	[[Category: Fatty acid biosynthesis]]		[[Category: Fatty acid biosynthesis]]
-	[[Category: Phosphopantetheine transferase]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:33:25 2009''

OCA at 08:33, 22 March 2009

2009-03-22T08:33:26Z

←Older revision		Revision as of 08:33, 22 March 2009
Line 12:		Line 12:
	===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A===		===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18022563}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18022563 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18022563}}

	==About this Structure==		==About this Structure==
	2C43 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA].		2C43 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C43 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:18022563</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: L-aminoadipate-semialdehyde dehydrogenase]]		[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
Line 32:		Line 41:
	[[Category: Fatty acid biosynthesis]]		[[Category: Fatty acid biosynthesis]]
	[[Category: Phosphopantetheine transferase]]		[[Category: Phosphopantetheine transferase]]
		+	[[Category: Transferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Feb 17 18~~:54:40 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:33:25 2009''