1w7m - Revision history

OCA at 13:19, 13 December 2023

2023-12-13T13:19:51Z

←Older revision		Revision as of 13:19, 13 December 2023
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	<StructureSection load='1w7m' size='340' side='right'caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1w7m' size='340' side='right'caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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]] 2.7Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1w7l\|1w7l]], [[1w7n\|1w7n]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13]~~ </~~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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [https://pdbe.org/1w7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [https://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7m 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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [https://pdbe.org/1w7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [https://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>	+	[https://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cysteine-S-conjugate beta-lyase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Han, Q]]	+	[[Category: Han Q]]
-	[[Category: Li, J]]	+	[[Category: Li J]]
-	[[Category: Rizzi, M]]	+	[[Category: Rizzi M]]
-	[[Category: Rossi, F]]	+	[[Category: Rossi F]]
-	~~[[Category: Aminotransferase]]~~	+
-	~~[[Category: Kynurenic acid]]~~	+
-	~~[[Category: Kynurenine pathway]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Multifunctional enzyme]]~~	+
-	~~[[Category: Plp-enzyme]]~~	+
-	~~[[Category: Pyridoxal phosphate]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:57, 26 May 2021

2021-05-26T09:57:23Z

←Older revision		Revision as of 09:57, 26 May 2021
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	<StructureSection load='1w7m' size='340' side='right'caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1w7m' size='340' side='right'caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1W7M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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=PHE:PHENYLALANINE'>PHE</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">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w7l\|1w7l]], [[1w7n\|1w7n]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [~~http~~://pdbe.org/1w7m PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7m 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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [https://pdbe.org/1w7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [https://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>	+	[[https://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:12, 21 August 2019

2019-08-21T07:12:30Z

←Older revision		Revision as of 07:12, 21 August 2019
Line 1:		Line 1:

	==Crystal structure of human kynurenine aminotransferase I in complex with L-Phe==		==Crystal structure of human kynurenine aminotransferase I in complex with L-Phe==
-	<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>	+	<StructureSection load='1w7m' size='340' side='right'caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>		<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/1w7m_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/1w7m_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 36:		Line 36:
	[[Category: Cysteine-S-conjugate beta-lyase]]		[[Category: Cysteine-S-conjugate beta-lyase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Han, Q]]		[[Category: Han, Q]]
	[[Category: Li, J]]		[[Category: Li, J]]

OCA at 17:28, 16 November 2017

2017-11-16T17:28:22Z

←Older revision		Revision as of 17:28, 16 November 2017
Line 1:		Line 1:
		+
	==Crystal structure of human kynurenine aminotransferase I in complex with L-Phe==		==Crystal structure of human kynurenine aminotransferase I in complex with L-Phe==
	<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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=PHE:PHENYLALANINE'>PHE</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">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://pdbe.org/1w7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m 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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://pdbe.org/1w7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 34:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Cysteine-S-conjugate beta-lyase]]		[[Category: Cysteine-S-conjugate beta-lyase]]
		+	[[Category: Human]]
	[[Category: Han, Q]]		[[Category: Han, Q]]
	[[Category: Li, J]]		[[Category: Li, J]]

OCA at 02:44, 10 February 2016

2016-02-10T02:44:24Z

←Older revision		Revision as of 02:44, 10 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=1w7m ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:30, 30 September 2015

2015-09-30T06:30:50Z

←Older revision		Revision as of 06:30, 30 September 2015
Line 1:		Line 1:
-	==~~CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE~~ I ~~IN COMPLEX WITH~~ L-~~PHE~~==	+	==Crystal structure of human kynurenine aminotransferase I in complex with L-Phe==
	<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~DPN~~:D-PHENYLALANINE'>~~DPN~~</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~LLP~~:~~2-LYSINE(3-HYDROXY-2-METHYL~~-5-~~PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)~~'>~~LLP~~</scene></td></tr>	+
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>
Line 35:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Cysteine-S-conjugate beta-lyase]]		[[Category: Cysteine-S-conjugate beta-lyase]]
-	[[Category: Homo sapiens]]
	[[Category: Han, Q]]		[[Category: Han, Q]]
	[[Category: Li, J]]		[[Category: Li, J]]

OCA at 04:35, 11 September 2015

2015-09-11T04:35:49Z

←Older revision		Revision as of 04:35, 11 September 2015
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m 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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://pdbe.org/1w7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m 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 1w7m" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:14, 25 December 2014

2014-12-25T11:14:17Z

←Older revision		Revision as of 11:14, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>		<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m 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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	[[Category: Cysteine-S-conjugate beta-lyase]]		[[Category: Cysteine-S-conjugate beta-lyase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Han, Q.]]	+	[[Category: Han, Q]]
-	[[Category: Li, J.]]	+	[[Category: Li, J]]
-	[[Category: Rizzi, M.]]	+	[[Category: Rizzi, M]]
-	[[Category: Rossi, F.]]	+	[[Category: Rossi, F]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Kynurenic acid]]		[[Category: Kynurenic acid]]

OCA at 18:25, 29 September 2014

2014-09-29T18:25:22Z

←Older revision		Revision as of 18:25, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1w7m.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE==
		+	<StructureSection load='1w7m' size='340' side='right' caption='[[1w7m]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1w7m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7M FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w7l\|1w7l]], [[1w7n\|1w7n]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB], [http://www.ebi.ac.uk/pdbsum/1w7m 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/w7/1w7m_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 ==
		+	The kynurenine pathway has long been regarded as a valuable target for the treatment of several neurological disorders accompanied by unbalanced levels of metabolites along the catabolic cascade, kynurenic acid among them. The irreversible transamination of kynurenine is the sole source of kynurenic acid, and it is catalyzed by different isoforms of the 5'-pyridoxal phosphate-dependent kynurenine aminotransferase (KAT). The KAT-I isozyme has also been reported to possess beta-lyase activity toward several sulfur- and selenium-conjugated molecules, leading to the proposal of a role of the enzyme in carcinogenesis associated with environmental pollutants. We solved the structure of human KAT-I in its 5'-pyridoxal phosphate and pyridoxamine phosphate forms and in complex with the competing substrate l-Phe. The enzyme active site revealed a striking crown of aromatic residues decorating the ligand binding pocket, which we propose as a major molecular determinant for substrate recognition. Ligand-induced conformational changes affecting Tyr(101) and the Trp(18)-bearing alpha-helix H1 appear to play a central role in catalysis. Our data reveal a key structural role of Glu(27), providing a molecular basis for the reported loss of enzymatic activity displayed by the equivalent Glu --> Gly mutation in KAT-I of spontaneously hypertensive rats.

-	~~{{STRUCTURE_1w7m\| PDB=1w7m \| SCENE= }}~~	+	Crystal structure of human kynurenine aminotransferase I.,Rossi F, Han Q, Li J, Li J, Rizzi M J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. PMID:15364907<ref>PMID:15364907</ref>

-	~~===CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15364907}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1w7m]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015364907<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Cysteine-S-conjugate beta-lyase]]		[[Category: Cysteine-S-conjugate beta-lyase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "1w7m" [edit=sysop:move=sysop]

2013-01-05T11:02:11Z

Protected "1w7m" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:02, 5 January 2013