2e48 - Revision history

OCA at 08:34, 25 October 2023

2023-10-25T08:34:40Z

←Older revision		Revision as of 08:34, 25 October 2023
Line 3:		Line 3:
	<StructureSection load='2e48' size='340' side='right'caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2e48' size='340' side='right'caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E48 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>~~</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]] 2.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</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></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3]~~ </~~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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [https://pdbe.org/2e48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [https://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [https://pdbe.org/2e48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [https://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>	+	[https://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~D-amino-acid oxidase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fukui, K]]	+	[[Category: Fukui K]]
-	[[Category: Imagawa, T]]	+	[[Category: Imagawa T]]
-	[[Category: Kawazoe, T]]	+	[[Category: Kawazoe T]]
-	[[Category: Tsuge, H]]	+	[[Category: Tsuge H]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Structurally ambivalent peptide]]~~	+
-	~~[[Category: Substrate-free holoenzyme~~]]	+

OCA at 17:20, 15 December 2021

2021-12-15T17:20:27Z

←Older revision		Revision as of 17:20, 15 December 2021
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	<StructureSection load='2e48' size='340' side='right'caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2e48' size='340' side='right'caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2E48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E48 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></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></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [~~http~~://pdbe.org/2e48 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [https://pdbe.org/2e48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [https://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>	+	[[https://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:27, 11 March 2020

2020-03-11T08:27:07Z

←Older revision		Revision as of 08:27, 11 March 2020
Line 1:		Line 1:

	==Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme==		==Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme==
-	<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='2e48' size='340' side='right'caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Amino acid oxidase\|Amino acid oxidase]]	+	*[[Amino acid oxidase 3D structures\|Amino acid oxidase 3D structures]]
	*[[Rossmann fold\|Rossmann fold]]		*[[Rossmann fold\|Rossmann fold]]
	== References ==		== References ==
Line 40:		Line 40:
	[[Category: D-amino-acid oxidase]]		[[Category: D-amino-acid oxidase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Fukui, K]]		[[Category: Fukui, K]]
	[[Category: Imagawa, T]]		[[Category: Imagawa, T]]

OCA at 07:10, 6 June 2018

2018-06-06T07:10:56Z

←Older revision		Revision as of 07:10, 6 June 2018
Line 1:		Line 1:
		+
	==Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme==		==Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme==
	<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://pdbe.org/2e48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://pdbe.org/2e48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/2e48_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/2e48_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 15:49, 9 February 2016

2016-02-09T15:49:29Z

←Older revision		Revision as of 15:49, 9 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e48 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:43, 10 September 2015

2015-09-10T23:43:56Z

←Older revision		Revision as of 23:43, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 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></td></tr>		</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></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://pdbe.org/2e48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 2e48" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: D-amino-acid oxidase]]		[[Category: D-amino-acid oxidase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Fukui, K]]		[[Category: Fukui, K]]
	[[Category: Imagawa, T]]		[[Category: Imagawa, T]]

OCA at 07:52, 25 December 2014

2014-12-25T07:52:10Z

←Older revision		Revision as of 07:52, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 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><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></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 31:
	==See Also==		==See Also==
	*[[Amino acid oxidase\|Amino acid oxidase]]		*[[Amino acid oxidase\|Amino acid oxidase]]
		+	*[[Rossmann fold\|Rossmann fold]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	[[Category: D-amino-acid oxidase]]		[[Category: D-amino-acid oxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Fukui, K.]]	+	[[Category: Fukui, K]]
-	[[Category: Imagawa, T.]]	+	[[Category: Imagawa, T]]
-	[[Category: Kawazoe, T.]]	+	[[Category: Kawazoe, T]]
-	[[Category: Tsuge, H.]]	+	[[Category: Tsuge, H]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Structurally ambivalent peptide]]		[[Category: Structurally ambivalent peptide]]
	[[Category: Substrate-free holoenzyme]]		[[Category: Substrate-free holoenzyme]]

OCA at 01:20, 30 September 2014

2014-09-30T01:20:53Z

←Older revision		Revision as of 01:20, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2e48.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme==
		+	<StructureSection load='2e48' size='340' side='right' caption='[[2e48]], [[Resolution\|resolution]] 2.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2e48]] is a 4 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 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><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2du8\|2du8]], [[2e49\|2e49]], [[2e4a\|2e4a]], [[2e82\|2e82]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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/e4/2e48_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 ==
		+	D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent endogenous ligand of N-methyl-D-aspartate type glutamate receptors. It also has been suggested that D-DOPA, the stereoisomer of L-DOPA, is oxidized by DAO and then converted to dopamine via an alternative biosynthetic pathway. Here, we provide direct crystallographic evidence that D-DOPA is readily fitted into the active site of human DAO, where it is oxidized by the enzyme. Moreover, our kinetic data show that the maximal velocity for oxidation of D-DOPA is much greater than for D-serine, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, determination of the structures of human DAO in various states revealed that the conformation of the hydrophobic VAAGL stretch (residues 47-51) to be uniquely stable in the human enzyme, which provides a structural basis for the unique kinetic features of human DAO.

-	~~{{STRUCTURE_2e48\| PDB=2e48 \| SCENE= }}~~	+	Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis.,Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. PMID:17303072<ref>PMID:17303072</ref>

-	~~===Crystal Structure~~ of ~~Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_17303072}}~~	+	==See Also==
-		+	*[[Amino acid oxidase\|Amino acid oxidase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~2e48~~]] is a 4 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=2E48 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:017303072<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: D-amino-acid oxidase]]		[[Category: D-amino-acid oxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "2e48" [edit=sysop:move=sysop]

2013-01-06T10:35:54Z

Protected "2e48" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:35, 6 January 2013

OCA at 10:35, 6 January 2013

2013-01-06T10:35:49Z

←Older revision		Revision as of 10:35, 6 January 2013
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-	{{Seed}}
	[[Image:2e48.png\|left\|200px]]		[[Image:2e48.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2e48", 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.
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	{{STRUCTURE_2e48\| PDB=2e48 \| SCENE= }}		{{STRUCTURE_2e48\| PDB=2e48 \| SCENE= }}

	===Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme===		===Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17303072}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17303072 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17303072}}		{{ABSTRACT_PUBMED_17303072}}

	==About this Structure==		==About this Structure==
-	~~2E48~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E48 OCA].	+	[[2e48]] is a 4 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=2E48 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17303072~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017303072</ref><references group="xtra"/>
	[[Category: D-amino-acid oxidase]]		[[Category: D-amino-acid oxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 30:		Line 18:
	[[Category: Kawazoe, T.]]		[[Category: Kawazoe, T.]]
	[[Category: Tsuge, H.]]		[[Category: Tsuge, H.]]
		+	[[Category: Oxidoreductase]]
	[[Category: Structurally ambivalent peptide]]		[[Category: Structurally ambivalent peptide]]
	[[Category: Substrate-free holoenzyme]]		[[Category: Substrate-free holoenzyme]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:57:29 2009''