2jb2 - Revision history

OCA at 14:41, 13 December 2023

OCA — Wed, 13 Dec 2023 14:41:07 GMT

←Older revision		Revision as of 14:41, 13 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</scene>~~, ~~<scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.45Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2]~~ </~~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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [https://pdbe.org/2jb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [https://pdbe.org/2jb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/OXLA_RHOOP OXLA_RHOOP] Catalyzes an oxidative deamination of basic, hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (Ref.1). Is active on most L-amino acid (39 on 43 tested) with the exception of L-Thr, L-Pro, and L-Gly (Ref.1).[PROSITE-ProRule:PRU00648]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: L-amino-acid oxidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Rhodococcus opacus]]		[[Category: Rhodococcus opacus]]
-	[[Category: Faust, A]]	+	[[Category: Faust A]]
-	[[Category: Hummel, W]]	+	[[Category: Hummel W]]
-	[[Category: Niefind, K]]	+	[[Category: Niefind K]]
-	[[Category: Schomburg, D]]	+	[[Category: Schomburg D]]
-	~~[[Category: Dimerisation mode]]~~	+
-	~~[[Category: Fad containing]]~~	+
-	~~[[Category: Flavoenzyme]]~~	+
-	~~[[Category: Gr2-family]]~~	+
-	~~[[Category: Hydride transfer mechanism]]~~	+
-	~~[[Category: L-amino acid oxidase]]~~	+
-	~~[[Category: Non-planar fad]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Substrate complex~~]]	+

OCA at 08:05, 19 January 2022

OCA — Wed, 19 Jan 2022 08:05:54 GMT

←Older revision		Revision as of 08:05, 19 January 2022
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	<StructureSection load='2jb2' size='340' side='right'caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='2jb2' size='340' side='right'caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [~~http~~://pdbe.org/2jb2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [https://pdbe.org/2jb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 07:45, 15 April 2020

OCA — Wed, 15 Apr 2020 07:45:49 GMT

←Older revision		Revision as of 07:45, 15 April 2020
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	==The structure of L-amino acid oxidase from Rhodococcus opacus in complex with L-phenylalanine.==		==The structure of L-amino acid oxidase from Rhodococcus opacus in complex with L-phenylalanine.==
-	<StructureSection load='2jb2' size='340' side='right' caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='2jb2' size='340' side='right'caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://pdbe.org/2jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://pdbe.org/2jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	==See Also==		==See Also==
-	*[[Amino acid oxidase\|Amino acid oxidase]]	+	*[[Amino acid oxidase 3D structures\|Amino acid oxidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: L-amino-acid oxidase]]		[[Category: L-amino-acid oxidase]]
		+	[[Category: Large Structures]]
	[[Category: Rhodococcus opacus]]		[[Category: Rhodococcus opacus]]
	[[Category: Faust, A]]		[[Category: Faust, A]]

OCA at 07:09, 11 July 2018

OCA — Wed, 11 Jul 2018 07:09:55 GMT

←Older revision		Revision as of 07:09, 11 July 2018
Line 1:		Line 1:
-	==~~THE STRUCTURE OF~~ L-~~AMINO ACID OXIDASE FROM RHODOCOCCUS OPACUS IN COMPLEX WITH~~ L-~~PHENYLALANINE~~.==	+
		+	==The structure of L-amino acid oxidase from Rhodococcus opacus in complex with L-phenylalanine.==
	<StructureSection load='2jb2' size='340' side='right' caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='2jb2' size='340' side='right' caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://pdbe.org/2jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://pdbe.org/2jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jb2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jb2_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 19:31, 7 February 2016

OCA — Sun, 07 Feb 2016 19:31:18 GMT

←Older revision		Revision as of 19:31, 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=2jb2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:23, 10 September 2015

OCA — Thu, 10 Sep 2015 04:23:18 GMT

←Older revision		Revision as of 04:23, 10 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://pdbe.org/2jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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 2jb2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 14:15, 19 January 2015

OCA — Mon, 19 Jan 2015 14:15:11 GMT

←Older revision		Revision as of 14:15, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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 35:		Line 35:
	[[Category: L-amino-acid oxidase]]		[[Category: L-amino-acid oxidase]]
	[[Category: Rhodococcus opacus]]		[[Category: Rhodococcus opacus]]
-	[[Category: Faust, A.]]	+	[[Category: Faust, A]]
-	[[Category: Hummel, W.]]	+	[[Category: Hummel, W]]
-	[[Category: Niefind, K.]]	+	[[Category: Niefind, K]]
-	[[Category: Schomburg, D.]]	+	[[Category: Schomburg, D]]
	[[Category: Dimerisation mode]]		[[Category: Dimerisation mode]]
	[[Category: Fad containing]]		[[Category: Fad containing]]

OCA at 02:35, 29 September 2014

OCA — Mon, 29 Sep 2014 02:35:47 GMT

←Older revision		Revision as of 02:35, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2jb2.~~png~~\|~~left~~\|200px]]	+	==THE STRUCTURE OF L-AMINO ACID OXIDASE FROM RHODOCOCCUS OPACUS IN COMPLEX WITH L-PHENYLALANINE.==
		+	<StructureSection load='2jb2' size='340' side='right' caption='[[2jb2]], [[Resolution\|resolution]] 1.45Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JB2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jae\|2jae]], [[2jb1\|2jb1]], [[2jb3\|2jb3]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=2jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2jb2 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/jb/2jb2_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 ==
		+	l-Amino acid oxidase from Rhodococcus opacus (roLAAO) is classified as a member of the GR(2)-family of flavin-dependent oxidoreductases according to a highly conserved sequence motif for the cofactor binding. The monomer of the homodimeric enzyme consists of three well-defined domains: the FAD-binding domain corresponding to a general topology throughout the whole GR(2)-family; a substrate-binding domain with almost the same topology as the snake venom LAAO and a helical domain exclusively responsible for the unusual dimerisation mode of the enzyme and not found in other members of the family so far. We describe here high-resolution structures of the binary complex of protein and cofactor as well as the ternary complexes of protein, cofactor and ligands. This structures in addition to the structural knowledge of snake venom LAAO and DAAO from yeast and pig kidney permit more insight into different steps in the reaction mechanism of this class of enzymes. There is strong evidence for hydride transfer as the mechanism of dehydrogenation. This mechanism appears to be uncommon in a sense that the chemical transformation can proceed efficiently without the involvement of amino acid functional groups. Most groups present at the active site are involved in substrate recognition, binding and fixation, i.e. they direct the trajectory of the interacting orbitals. In this mode of catalysis orbital steering/interactions are the predominant factors for the chemical step(s). A mirror-symmetrical relationship between the two substrate-binding sites of d and l-amino acid oxidases is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the residues in the active site. These results are of general relevance for the mechanism of flavoproteins and lead to the proposal of a common dehydrogenation step in the mechanism for l and d-amino acid oxidases.

-	~~{{STRUCTURE_2jb2\| PDB=2jb2 \| SCENE= }}~~	+	The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation.,Faust A, Niefind K, Hummel W, Schomburg D J Mol Biol. 2007 Mar 16;367(1):234-48. Epub 2006 Dec 1. PMID:17234209<ref>PMID:17234209</ref>

-	~~===THE STRUCTURE OF L-AMINO ACID OXIDASE FROM RHODOCOCCUS OPACUS IN COMPLEX WITH L-PHENYLALANINE.===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17234209}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2jb2]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rhodococcus_opacus Rhodococcus opacus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA].~~	+

	==See Also==		==See Also==
	*[[Amino acid oxidase\|Amino acid oxidase]]		*[[Amino acid oxidase\|Amino acid oxidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017234209<~~/~~ref~~><~~ref group="xtra">PMID:016511322</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: L-amino-acid oxidase]]		[[Category: L-amino-acid oxidase]]
	[[Category: Rhodococcus opacus]]		[[Category: Rhodococcus opacus]]

OCA at 07:38, 20 October 2012

OCA — Sat, 20 Oct 2012 07:38:54 GMT

←Older revision		Revision as of 07:38, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2jb2]] is a 2 chain structure ~~of [[Amino acid oxidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA].	+	[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA].

	==See Also==		==See Also==

OCA at 16:59, 25 July 2012

OCA — Wed, 25 Jul 2012 16:59:48 GMT

←Older revision		Revision as of 16:59, 25 July 2012
Line 1:		Line 1:
	[[Image:2jb2.png\|left\|200px]]		[[Image:2jb2.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2jb2\| PDB=2jb2 \| SCENE= }}		{{STRUCTURE_2jb2\| PDB=2jb2 \| SCENE= }}

	===THE STRUCTURE OF L-AMINO ACID OXIDASE FROM RHODOCOCCUS OPACUS IN COMPLEX WITH L-PHENYLALANINE.===		===THE STRUCTURE OF L-AMINO ACID OXIDASE FROM RHODOCOCCUS OPACUS IN COMPLEX WITH L-PHENYLALANINE.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17234209}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17234209 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_17234209}}		{{ABSTRACT_PUBMED_17234209}}

	==About this Structure==		==About this Structure==
-	[[2jb2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA].	+	[[2jb2]] is a 2 chain structure of [[Amino acid oxidase]] with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JB2 OCA].
		+
		+	==See Also==
		+	*[[Amino acid oxidase\|Amino acid oxidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17234209~~</ref><ref group="xtra">PMID:~~16511322~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017234209</ref><ref group="xtra">PMID:016511322</ref><references group="xtra"/>
	[[Category: L-amino-acid oxidase]]		[[Category: L-amino-acid oxidase]]
	[[Category: Rhodococcus opacus]]		[[Category: Rhodococcus opacus]]