1uu2 - Revision history

OCA at 12:58, 13 December 2023

2023-12-13T12:58:47Z

←Older revision		Revision as of 12:58, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1uu2' size='340' side='right'caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1uu2' size='340' side='right'caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_43589 Atcc 43589~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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]] 2.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidinol~~-~~phosphate_transaminase Histidinol~~-~~phosphate transaminase], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9]~~ </~~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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [https://pdbe.org/1uu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1uu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu2 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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [https://pdbe.org/1uu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1uu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu2 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/HIS8_THEMA HIS8_THEMA]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43589]]
-	[[Category: Histidinol-phosphate transaminase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Fernandez, F J~~]]	+	[[Category: Thermotoga maritima]]
-	[[Category: ~~Lehmann, F~~]]	+	[[Category: Fernandez FJ]]
-	[[Category: ~~Vega, M C~~]]	+	[[Category: Lehmann F]]
-	[[Category: ~~Wilmanns, M~~]]	+	[[Category: Vega MC]]
-	[[Category: ~~Aminotransferase]]~~	+	[[Category: Wilmanns M]]
-	~~[[Category: Complete proteome aminotransferase]]~~	+
-	~~[[Category: Histidine biosynthesis]]~~	+
-	~~[[Category: Pyridoxal phosphate]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:05, 28 April 2021

2021-04-28T06:05:17Z

←Older revision		Revision as of 06:05, 28 April 2021
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	<StructureSection load='1uu2' size='340' side='right'caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1uu2' size='340' side='right'caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [~~http~~://pdbe.org/1uu2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1uu2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu2 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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [https://pdbe.org/1uu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1uu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu2 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 07:04, 24 July 2019

2019-07-24T07:04:49Z

←Older revision		Revision as of 07:04, 24 July 2019
Line 1:		Line 1:

	==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (apo-form)==		==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (apo-form)==
-	<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1uu2' size='340' side='right'caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Aminotransferase\|Aminotransferase]]	+	*[[Aminotransferase 3D structures\|Aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	[[Category: Atcc 43589]]		[[Category: Atcc 43589]]
	[[Category: Histidinol-phosphate transaminase]]		[[Category: Histidinol-phosphate transaminase]]
		+	[[Category: Large Structures]]
	[[Category: Fernandez, F J]]		[[Category: Fernandez, F J]]
	[[Category: Lehmann, F]]		[[Category: Lehmann, F]]

OCA at 07:44, 28 March 2018

2018-03-28T07:44:14Z

←Older revision		Revision as of 07:44, 28 March 2018
Line 1:		Line 1:
-	==~~HISTIDINOL~~-~~PHOSPHATE AMINOTRANSFERASE~~ (~~HISC~~) ~~FROM THERMOTOGA MARITIMA~~ (~~APO~~-~~FORM~~)==	+
		+	==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (apo-form)==
	<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://pdbe.org/1uu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://pdbe.org/1uu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu2 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/1uu2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/1uu2_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 18:25, 7 February 2016

2016-02-07T18:25:29Z

←Older revision		Revision as of 18:25, 7 February 2016
Line 16:		Line 16:
	<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=1uu2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1uu2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1uu2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminotransferase\|Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:01, 10 September 2015

2015-09-10T04:01:32Z

←Older revision		Revision as of 04:01, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermotoga_maritima Thermotoga maritima~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://pdbe.org/1uu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 26:
	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 1uu2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 43589]]
	[[Category: Histidinol-phosphate transaminase]]		[[Category: Histidinol-phosphate transaminase]]
-	[[Category: Thermotoga maritima]]
	[[Category: Fernandez, F J]]		[[Category: Fernandez, F J]]
	[[Category: Lehmann, F]]		[[Category: Lehmann, F]]

OCA at 12:32, 6 January 2015

2015-01-06T12:32:56Z

←Older revision		Revision as of 12:32, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	[[Category: Histidinol-phosphate transaminase]]		[[Category: Histidinol-phosphate transaminase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
-	[[Category: Fernandez, F J.]]	+	[[Category: Fernandez, F J]]
-	[[Category: Lehmann, F.]]	+	[[Category: Lehmann, F]]
-	[[Category: Vega, M C.]]	+	[[Category: Vega, M C]]
-	[[Category: Wilmanns, M.]]	+	[[Category: Wilmanns, M]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Complete proteome aminotransferase]]		[[Category: Complete proteome aminotransferase]]

OCA at 18:27, 29 September 2014

2014-09-29T18:27:56Z

←Older revision		Revision as of 18:27, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1uu2.~~png~~\|~~left~~\|200px]]	+	==HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)==
		+	<StructureSection load='1uu2' size='340' side='right' caption='[[1uu2]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1uu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UU2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h1c\|1h1c]], [[1uu0\|1uu0]], [[1uu1\|1uu1]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=1uu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uu2 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/uu/1uu2_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 ==
		+	In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes the transfer of the amino group from glutamate to imidazole acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In some organisms such as the hyperthermophile Thermotoga maritima, specific tyrosine and aromatic amino acid transaminases have not been identified to date, suggesting an additional role for histidinol-phosphate aminotransferase in other transamination reactions generating aromatic amino acids. To gain insight into the specific function of this transaminase, we have determined its crystal structure in the absence of any ligand except phosphate, in the presence of covalently bound pyridoxal 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of pyridoxamine 5'-phosphate. The enzyme accepts histidinol phosphate, tyrosine, tryptophan, and phenylalanine, but not histidine, as substrates. The structures provide a model of how these different substrates could be accommodated by histidinol-phosphate aminotransferase. Some of the structural features of the enzyme are more preserved between the T. maritima enzyme and a related threonine-phosphate decarboxylase from S. typhimurium than with histidinol-phosphate aminotransferases from different organisms.

-	~~{{STRUCTURE_1uu2\| PDB=1uu2 \| SCENE= }}~~	+	Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.,Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M J Biol Chem. 2004 May 14;279(20):21478-88. Epub 2004 Mar 8. PMID:15007066<ref>PMID:15007066</ref>

-	~~===HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15007066}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1uu2]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermotoga_maritima Thermotoga maritima]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1UU2 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015007066<~~/~~ref~~><~~ref group="xtra">PMID:011518529</ref><references group="xtra"~~/>	+
	[[Category: Histidinol-phosphate transaminase]]		[[Category: Histidinol-phosphate transaminase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]

OCA at 09:41, 16 January 2013

2013-01-16T09:41:24Z

←Older revision		Revision as of 09:41, 16 January 2013
Line 1:		Line 1:
	[[Image:1uu2.png\|left\|200px]]		[[Image:1uu2.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1uu2", 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_1uu2\| PDB=1uu2 \| SCENE= }}		{{STRUCTURE_1uu2\| PDB=1uu2 \| SCENE= }}

	===HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)===		===HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15007066}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15007066 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15007066}}		{{ABSTRACT_PUBMED_15007066}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15007066~~</ref><ref group="xtra">PMID:~~11518529~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015007066</ref><ref group="xtra">PMID:011518529</ref><references group="xtra"/>
	[[Category: Histidinol-phosphate transaminase]]		[[Category: Histidinol-phosphate transaminase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]

OCA: Protected "1uu2" [edit=sysop:move=sysop]

2011-03-14T18:16:04Z

Protected "1uu2" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:16, 14 March 2011