3i9u - Revision history

OCA at 15:56, 1 November 2023

OCA — Wed, 01 Nov 2023 15:56:47 GMT

←Older revision		Revision as of 15:56, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3i9u' size='340' side='right'caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='3i9u' size='340' side='right'caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I9U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I9U FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=DTU:(2R,3S)~~-1,~~4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.25Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3i9t\|3i9t]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>Hmox1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~10116 Buffalo rat])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3]~~ </~~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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [https://pdbe.org/3i9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [https://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u 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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [https://pdbe.org/3i9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [https://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.	+	[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
-	[[Category: Heme oxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ikeda-Saito, M]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Matsui, T]]	+	[[Category: Ikeda-Saito M]]
-	[[Category: Unno, M]]	+	[[Category: Matsui T]]
-	~~[[Category: Endoplasmic reticulum]]~~	+	[[Category: Unno M]]
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Isozyme]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Microsome]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phosphoprotein~~]]	+

OCA at 11:01, 13 April 2022

OCA — Wed, 13 Apr 2022 11:01:41 GMT

←Older revision		Revision as of 11:01, 13 April 2022
Line 1:		Line 1:

	==Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)==		==Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)==
-	<StructureSection load='3i9u' size='340' side='right' caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='3i9u' size='340' side='right'caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3I9U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I9U FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i9t\|3i9t]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3i9t\|3i9t]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [~~http~~://pdbe.org/3i9u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u 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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [https://pdbe.org/3i9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [https://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.	+	[[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Heme oxygenase\|Heme oxygenase]]	+	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Ikeda-Saito, M]]		[[Category: Ikeda-Saito, M]]
	[[Category: Matsui, T]]		[[Category: Matsui, T]]

OCA at 09:51, 19 December 2018

OCA — Wed, 19 Dec 2018 09:51:06 GMT

←Older revision		Revision as of 09:51, 19 December 2018
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/3i9u_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/3i9u_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 17:31, 4 August 2016

OCA — Thu, 04 Aug 2016 17:31:42 GMT

←Older revision		Revision as of 17:31, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)==		==Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)==
	<StructureSection load='3i9u' size='340' side='right' caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='3i9u' size='340' side='right' caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I9U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I9U FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i9t\|3i9t]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i9t\|3i9t]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [http://www.ebi.ac.uk/pdbsum/3i9u 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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [http://pdbe.org/3i9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [http://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=3i9u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3i9u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
-	[[Category: Rattus norvegicus]]
	[[Category: Ikeda-Saito, M]]		[[Category: Ikeda-Saito, M]]
	[[Category: Matsui, T]]		[[Category: Matsui, T]]

OCA at 11:26, 25 December 2014

OCA — Thu, 25 Dec 2014 11:26:09 GMT

←Older revision		Revision as of 11:26, 25 December 2014
Line 9:		Line 9:
	<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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [http://www.ebi.ac.uk/pdbsum/3i9u 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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [http://www.ebi.ac.uk/pdbsum/3i9u PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:20, 8 December 2014

OCA — Mon, 08 Dec 2014 09:20:19 GMT

←Older revision		Revision as of 09:20, 8 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3i9u.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)==
		+	<StructureSection load='3i9u' size='340' side='right' caption='[[3i9u]], [[Resolution\|resolution]] 2.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I9U FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i9t\|3i9t]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [http://www.ebi.ac.uk/pdbsum/3i9u 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/i9/3i9u_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 ==
		+	Heme oxygenase (HO) catalyzes the regiospecific conversion of heme to biliverdin, CO, and free iron through three successive oxygenation reactions. HO catalysis is unique in that all three O(2) activations are performed by the substrate itself. This Forum Article overviews our current understanding on the structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps. The HO first step, regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, is of particular interest because of its sharp contrast to O(2) activation by cytochrome P450. HO was proposed to utilize the FeOOH species but not conventional ferryl hemes as a reactive intermediate for self-hydroxylation. We have succeeded in preparing and characterizing the FeOOH species of HO at low temperature, and our analyses of its reaction, together with mutational and crystallographic studies, reveal that protonation of FeOOH by a distal water molecule is critical in promoting the unique self-hydroxylation. The second oxygenation is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. Further O(2) activation by verdoheme cleaves its porphyrin macrocycle to form biliverdin and free ferrous iron. This third step has been considered to be a major rate-determining step of HO catalysis to regulate the enzyme activity. Our reaction analysis strongly supports the FeOOH verdoheme as the key intermediate of the ring-opening reaction. This mechanism is very similar to that of the first meso-hydroxylation, and the distal water is suggested to enhance the third step as expected from the similarity. The HO mechanistic studies highlight the catalytic importance of the distal hydrogen-bonding network, and this manuscript also involves our attempts to develop HO inhibitors targeting the unique distal structure.

-	~~{{STRUCTURE_3i9u\| PDB=3i9u \| SCENE= }}~~	+	Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase.,Matsui T, Iwasaki M, Sugiyama R, Unno M, Ikeda-Saito M Inorg Chem. 2010 Apr 19;49(8):3602-9. PMID:20380462<ref>PMID:20380462</ref>

-	~~===Crystal structure~~ of the ~~rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20380462}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3i9u]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].~~	+

	==See Also==		==See Also==
	*[[Heme oxygenase\|Heme oxygenase]]		*[[Heme oxygenase\|Heme oxygenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020380462<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Ikeda-Saito, M.]]	+	[[Category: Ikeda-Saito, M]]
-	[[Category: Matsui, T.]]	+	[[Category: Matsui, T]]
-	[[Category: Unno, M.]]	+	[[Category: Unno, M]]
	[[Category: Endoplasmic reticulum]]		[[Category: Endoplasmic reticulum]]
	[[Category: Heme]]		[[Category: Heme]]
-	[[Category: Heme oxygenase]]
	[[Category: Inhibitor]]		[[Category: Inhibitor]]
	[[Category: Iron]]		[[Category: Iron]]

OCA at 16:09, 20 October 2012

OCA — Sat, 20 Oct 2012 16:09:05 GMT

←Older revision		Revision as of 16:09, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3i9u]] is a 1 chain structure ~~of [[Heme oxygenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].	+	[[3i9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].

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

OCA: Protected "3i9u" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 20:45:35 GMT

Protected "3i9u" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:45, 26 July 2012

OCA at 20:45, 26 July 2012

OCA — Thu, 26 Jul 2012 20:45:32 GMT

←Older revision		Revision as of 20:45, 26 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3i9u.png\|left\|200px]]
-	[[Image:3i9u.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3i9u", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3i9u\| PDB=3i9u \| SCENE= }}		{{STRUCTURE_3i9u\| PDB=3i9u \| SCENE= }}

	===Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)===		===Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20380462}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20380462 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20380462}}		{{ABSTRACT_PUBMED_20380462}}

	==About this Structure==		==About this Structure==
-	~~3I9U~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].	+	[[3i9u]] is a 1 chain structure of [[Heme oxygenase]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].
		+
		+	==See Also==
		+	*[[Heme oxygenase\|Heme oxygenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20380462~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020380462</ref><references group="xtra"/>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 39:		Line 30:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:33:31 2010''

OCA at 06:33, 20 May 2010

OCA — Thu, 20 May 2010 06:33:32 GMT

←Older revision		Revision as of 06:33, 20 May 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3i9u.jpg\|left\|200px]]

-	The ~~entry 3i9u~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3i9u", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3i9u\| PDB=3i9u \| SCENE= }}

-	~~Authors: Matsui, T., Unno, M., Ikeda~~-~~Saito, M.~~	+	===Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)===

-	Description: Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Aug 5~~ 09:49:~~05 2009~~''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20380462}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20380462 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20380462}}
		+
		+	==About this Structure==
		+	3I9U is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I9U OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20380462</ref><references group="xtra"/>
		+	[[Category: Heme oxygenase]]
		+	[[Category: Rattus norvegicus]]
		+	[[Category: Ikeda-Saito, M.]]
		+	[[Category: Matsui, T.]]
		+	[[Category: Unno, M.]]
		+	[[Category: Endoplasmic reticulum]]
		+	[[Category: Heme]]
		+	[[Category: Heme oxygenase]]
		+	[[Category: Inhibitor]]
		+	[[Category: Iron]]
		+	[[Category: Isozyme]]
		+	[[Category: Metal-binding]]
		+	[[Category: Microsome]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Phosphoprotein]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:33:31 2010''