2hgw - Revision history

OCA at 07:39, 17 March 2021

OCA — Wed, 17 Mar 2021 07:39:43 GMT

←Older revision		Revision as of 07:39, 17 March 2021
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	==Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase==		==Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase==
-	<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>	+	<StructureSection load='2hgw' size='340' side='right'caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2HGW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HGW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [~~http~~://pdbe.org/2hgw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2hgw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2hgw 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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [https://pdbe.org/2hgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [https://www.ebi.ac.uk/pdbsum/2hgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hgw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BCAT2_HUMAN BCAT2_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.	+	[[https://www.uniprot.org/uniprot/BCAT2_HUMAN BCAT2_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/2hgw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/2hgw_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Aminotransferase\|Aminotransferase]]	+	*[[Aminotransferase 3D structures\|Aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hutson, S M]]		[[Category: Hutson, S M]]
	[[Category: Yennawar, N H]]		[[Category: Yennawar, N H]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:11, 18 October 2017

OCA — Wed, 18 Oct 2017 08:11:59 GMT

←Older revision		Revision as of 08:11, 18 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase==		==Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase==
	<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>		<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://pdbe.org/2hgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw 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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://pdbe.org/2hgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hgw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 00:41, 9 February 2016

OCA — Tue, 09 Feb 2016 00:41:45 GMT

←Older revision		Revision as of 00:41, 9 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hgw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2hgw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2hgw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminotransferase\|Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:55, 10 September 2015

OCA — Thu, 10 Sep 2015 16:55:54 GMT

←Older revision		Revision as of 16:55, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>		<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HGW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HGW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw 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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://pdbe.org/2hgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	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 2hgw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hutson, S M]]		[[Category: Hutson, S M]]
	[[Category: Yennawar, N H]]		[[Category: Yennawar, N H]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 03:16, 25 December 2014

OCA — Thu, 25 Dec 2014 03:16:19 GMT

←Older revision		Revision as of 03:16, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HGW FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HGW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw 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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BCAT2_HUMAN BCAT2_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hutson, S M.]]	+	[[Category: Hutson, S M]]
-	[[Category: Yennawar, N H.]]	+	[[Category: Yennawar, N H]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:33, 30 September 2014

OCA — Tue, 30 Sep 2014 08:33:22 GMT

←Older revision		Revision as of 08:33, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2hgw.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase==
		+	<StructureSection load='2hgw' size='340' side='right' caption='[[2hgw]], [[Resolution\|resolution]] 1.98Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2hgw]] 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=2HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HGW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ekf\|1ekf]], [[1ekp\|1ekp]], [[1ekv\|1ekv]], [[1kta\|1kta]], [[1kt8\|1kt8]], [[2a1h\|2a1h]], [[2hdk\|2hdk]], [[2hg8\|2hg8]], [[2hgx\|2hgx]], [[2hhf\|2hhf]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hgw RCSB], [http://www.ebi.ac.uk/pdbsum/2hgw 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/hg/2hgw_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 ==
		+	Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein. The N-terminal loop between residues 15 and 32 is flexible in the oxidized and mutant enzymes, the disorder greater in the oxidized protein. Disordering of the N-terminal loop disrupts the integrity of the side chain binding pocket, particularly for the branched chain side chain, less so for the dicarboxylate substrate side chain. The kinetic studies of the mutant and oxidized enzymes support the structural analysis. The kinetic results showed that the predominant effect of oxidation was on the second half-reaction rather than the first half-reaction. The oxidized enzyme was completely inactive, whereas the mutants showed limited activity. Model building of the second half-reaction substrate alpha-ketoisocaproate in the pyridoxamine 5'-phosphate-hBCATm structure suggests that disruption of the CXXC center results in altered substrate orientation and deprotonation of the amino group of pyridoxamine 5'-phosphate, which inhibits catalysis.

-	~~{{STRUCTURE_2hgw\| PDB=2hgw \| SCENE= }}~~	+	Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis.,Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. PMID:17050531<ref>PMID:17050531</ref>

-	~~===Crystal structure~~ of ~~Cys318Ala mutant of human mitochondrial branched chain aminotransferase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17050531}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2hgw]] 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=2HGW OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:017050531<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

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

OCA — Mon, 07 Jan 2013 10:57:15 GMT

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

←Older revision

Revision as of 10:57, 7 January 2013

OCA at 10:57, 7 January 2013

OCA — Mon, 07 Jan 2013 10:57:10 GMT

←Older revision		Revision as of 10:57, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2hgw.png\|left\|200px]]		[[Image:2hgw.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2hgw", 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_2hgw\| PDB=2hgw \| SCENE= }}		{{STRUCTURE_2hgw\| PDB=2hgw \| SCENE= }}

	===Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase===		===Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17050531}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17050531 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17050531}}		{{ABSTRACT_PUBMED_17050531}}

	==About this Structure==		==About this Structure==
-	~~2HGW~~ 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=2HGW OCA].	+	[[2hgw]] 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=2HGW OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17050531~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017050531</ref><references group="xtra"/>
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 29:		Line 17:
	[[Category: Yennawar, N H.]]		[[Category: Yennawar, N H.]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 04:58:03 2009''~~	+

OCA at 02:58, 17 February 2009

OCA — Tue, 17 Feb 2009 02:58:04 GMT

←Older revision		Revision as of 02:58, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2HGW is a ~~[[Single protein]]~~ 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=2HGW OCA].	+	2HGW 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=2HGW OCA].

	==Reference==		==Reference==
-	Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis., Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM, J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/17050531 17050531]~~	+	<ref group="xtra">PMID:17050531</ref><references group="xtra"/>
	[[Category: Branched-chain-amino-acid transaminase]]		[[Category: Branched-chain-amino-acid transaminase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Hutson, S M.]]		[[Category: Hutson, S M.]]
	[[Category: Yennawar, N H.]]		[[Category: Yennawar, N H.]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 08~~:21:~~51 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:58:03 2009''

OCA at 05:21, 28 July 2008

OCA — Mon, 28 Jul 2008 05:21:54 GMT

←Older revision		Revision as of 05:21, 28 July 2008
Line 1:		Line 1:
-	[[Image:2hgw.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2hgw.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_2hgw\| PDB=2hgw \| SCENE= }}		{{STRUCTURE_2hgw\| PDB=2hgw \| SCENE= }}

-	~~'''~~Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase~~'''~~	+	===Crystal structure of Cys318Ala mutant of human mitochondrial branched chain aminotransferase===


-	~~==Overview==~~	+	<!--
-	~~Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A~~, ~~C318A~~, ~~and C315A/C318A) of human mitochondrial (hBCATm) isozyme and~~ the ~~oxidized hBCATm enzyme (hBCATm-Ox) have been used~~ to ~~elucidate~~ the ~~role of this center in hBCATm catalysis~~. ~~X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis~~. ~~In all structures~~, ~~there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein. The N-terminal loop between residues 15 and 32~~ is ~~flexible in~~ the ~~oxidized and mutant enzymes, the disorder greater in the oxidized protein~~. ~~Disordering of the N~~-terminal loop disrupts the integrity of the side chain binding pocket, particularly for the branched chain side chain, less so for the dicarboxylate substrate side chain. The kinetic studies of the mutant and oxidized enzymes support the structural analysis. The kinetic results showed that the predominant effect of oxidation was on the second half-reaction rather than the first half-reaction. The oxidized enzyme was completely inactive, whereas the mutants showed limited activity. Model building of the second half-reaction substrate alpha-ketoisocaproate in the pyridoxamine 5'-phosphate-hBCATm structure suggests that disruption of the CXXC center results in altered substrate orientation and deprotonation of the amino group of pyridoxamine 5'-phosphate, which inhibits catalysis.	+	The line below this paragraph, {{ABSTRACT_PUBMED_17050531}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 17050531 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_17050531}}

	==About this Structure==		==About this Structure==
Line 26:		Line 30:
	[[Category: Yennawar, N H.]]		[[Category: Yennawar, N H.]]
	[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]		[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 06~~:16:49 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:21:51 2008''