2cog - Revision history

OCA at 11:27, 22 May 2024

2024-05-22T11:27:44Z

←Older revision		Revision as of 11:27, 22 May 2024
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	<StructureSection load='2cog' size='340' side='right'caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2cog' size='340' side='right'caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=4MV:4~~-~~METHYL+VALERIC+ACID'>4MV</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.1Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2coi\|2coi]], [[2coj\|2coj]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Branched~~-~~chain~~-~~amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42]~~ </~~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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [https://pdbe.org/2cog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [https://www.ebi.ac.uk/pdbsum/2cog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cog 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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [https://pdbe.org/2cog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [https://www.ebi.ac.uk/pdbsum/2cog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BCAT1_HUMAN BCAT1_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.	+	[https://www.uniprot.org/uniprot/BCAT1_HUMAN BCAT1_HUMAN] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
	== 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: ~~Branched-chain-amino-acid transaminase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Goto, M]]	+	[[Category: Goto M]]
-	~~[[Category: Plp-dependent enzyme]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:47, 10 November 2021

2021-11-10T06:47:01Z

←Older revision		Revision as of 06:47, 10 November 2021
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	<StructureSection load='2cog' size='340' side='right'caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2cog' size='340' side='right'caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2COG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2coi\|2coi]], [[2coj\|2coj]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [~~http~~://pdbe.org/2cog PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2cog PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2cog 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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [https://pdbe.org/2cog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [https://www.ebi.ac.uk/pdbsum/2cog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BCAT1_HUMAN BCAT1_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.	+	[[https://www.uniprot.org/uniprot/BCAT1_HUMAN BCAT1_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:49, 26 February 2020

2020-02-26T10:49:38Z

←Older revision		Revision as of 10:49, 26 February 2020
Line 1:		Line 1:

	==Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate==		==Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate==
-	<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='2cog' size='340' side='right'caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>
Line 36:		Line 36:
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Goto, M]]		[[Category: Goto, M]]
	[[Category: Plp-dependent enzyme]]		[[Category: Plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:06, 23 May 2018

2018-05-23T08:06:02Z

←Older revision		Revision as of 08:06, 23 May 2018
Line 1:		Line 1:
		+
	==Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate==		==Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate==
	<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://pdbe.org/2cog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog 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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://pdbe.org/2cog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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/co/2cog_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/2cog_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>

OCA at 09:08, 9 February 2016

2016-02-09T09:08:27Z

←Older revision		Revision as of 09:08, 9 February 2016
Line 18:		Line 18:
	<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=2cog ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:44, 10 September 2015

2015-09-10T20:44:56Z

←Older revision		Revision as of 20:44, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog 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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://pdbe.org/2cog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog 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 2cog" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Goto, M]]		[[Category: Goto, M]]
	[[Category: Plp-dependent enzyme]]		[[Category: Plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 05:55, 25 December 2014

2014-12-25T05:55:48Z

←Older revision		Revision as of 05:55, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog 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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BCAT1_HUMAN BCAT1_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Goto, M.]]	+	[[Category: Goto, M]]
	[[Category: Plp-dependent enzyme]]		[[Category: Plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 01:38, 30 September 2014

2014-09-30T01:38:29Z

←Older revision		Revision as of 01:38, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2cog.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate==
		+	<StructureSection load='2cog' size='340' side='right' caption='[[2cog]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2cog]] is a 2 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=2COG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MV:4-METHYL+VALERIC+ACID'>4MV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2coi\|2coi]], [[2coj\|2coj]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cog RCSB], [http://www.ebi.ac.uk/pdbsum/2cog 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/co/2cog_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	This study presents the first three-dimensional structures of human cytosolic branched-chain aminotransferase (hBCATc) isozyme complexed with the neuroactive drug gabapentin, the hBCATc Michaelis complex with the substrate analog, 4-methylvalerate, and the mitochondrial isozyme (hBCATm) complexed with gabapentin. The branched-chain aminotransferases (BCAT) reversibly catalyze transamination of the essential branched-chain amino acids (leucine, isoleucine, valine) to alpha-ketoglutarate to form the respective branched-chain alpha-keto acids and glutamate. The cytosolic isozyme is the predominant BCAT found in the nervous system, and only hBCATc is inhibited by gabapentin. Pre-steady state kinetics show that 1.3 mm gabapentin can completely inhibit the binding of leucine to reduced hBCATc, whereas 65.4 mm gabapentin is required to inhibit leucine binding to hBCATm. Structural analysis shows that the bulky gabapentin is enclosed in the active-site cavity by the shift of a flexible loop that enlarges the active-site cavity. The specificity of gabapentin for the cytosolic isozyme is ascribed at least in part to the location of the interdomain loop and the relative orientation between the small and large domain which is different from these relationships in the mitochondrial isozyme. Both isozymes contain a CXXC center and form a disulfide bond under oxidizing conditions. The structure of reduced hBCATc was obtained by soaking the oxidized hBCATc crystals with dithiothreitol. The close similarity in active-site structures between cytosolic enzyme complexes in the oxidized and reduced states is consistent with the small effect of oxidation on pre-steady state kinetics of the hBCATc first half-reaction. However, these kinetic data do not explain the inactivation of hBCATm by oxidation of the CXXC center. The structural data suggest that there is a larger effect of oxidation on the interdomain loop and residues surrounding the CXXC center in hBCATm than in hBCATc.

-	~~{{STRUCTURE_2cog\| PDB=2cog \| SCENE= }}~~	+	Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin.,Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. PMID:16141215<ref>PMID:16141215</ref>

-	~~===Crystal structure~~ of ~~oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16141215}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2cog]] is a 2 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=2COG OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016141215<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

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

2013-01-06T10:53:27Z

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

←Older revision

Revision as of 10:53, 6 January 2013

OCA at 10:53, 6 January 2013

2013-01-06T10:53:24Z

←Older revision		Revision as of 10:53, 6 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2cog.png\|left\|200px]]		[[Image:2cog.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2cog", 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_2cog\| PDB=2cog \| SCENE= }}		{{STRUCTURE_2cog\| PDB=2cog \| SCENE= }}

	===Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate===		===Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16141215}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16141215 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16141215}}		{{ABSTRACT_PUBMED_16141215}}

	==About this Structure==		==About this Structure==
-	~~2COG~~ is a 2 ~~chains~~ structure ~~of sequences~~ 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=2COG OCA].	+	[[2cog]] is a 2 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=2COG OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16141215~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016141215</ref><references group="xtra"/>
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Goto, M.]]		[[Category: Goto, M.]]
	[[Category: Plp-dependent enzyme]]		[[Category: Plp-dependent enzyme]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 08:39:00 2009''~~	+