1s13 - Revision history

OCA at 06:11, 23 August 2023

OCA — Wed, 23 Aug 2023 06:11:11 GMT

←Older revision		Revision as of 06:11, 23 August 2023
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	<StructureSection load='1s13' size='340' side='right'caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>		<StructureSection load='1s13' size='340' side='right'caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1S13 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S13 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=2FH:~~2~~-PHENYLHEME'>2FH</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]] 2.29Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [https://pdbe.org/1s13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [https://www.ebi.ac.uk/pdbsum/1s13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s13 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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [~~http~~://pdbe.org/1s13 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1s13 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1s13 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[~~http~~://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>	+	[https://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[https://omim.org/entry/614034 614034]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] 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_HUMAN HMOX1_HUMAN] 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]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Heme oxygenase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Buldain, G]]	+	[[Category: Buldain G]]
-	[[Category: Lad, L]]	+	[[Category: Lad L]]
-	[[Category: ~~Montellano, P R.Ortiz de~~]]	+	[[Category: Niemevz F]]
-	[[Category: ~~Niemevz, F~~]]	+	[[Category: Ortiz de Montellano PR]]
-	[[Category: Poulos~~, T L~~]]	+	[[Category: Poulos TL]]
-	[[Category: Wang, J]]	+	[[Category: Wang J]]
-	~~[[Category: Heme degradation]]~~	+
-	~~[[Category: Heme oxygenase-1]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 13:37, 16 December 2020

OCA — Wed, 16 Dec 2020 13:37:50 GMT

←Older revision		Revision as of 13:37, 16 December 2020
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	==Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes==		==Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes==
-	<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>	+	<StructureSection load='1s13' size='340' side='right'caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1S13 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S13 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://pdbe.org/1s13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s13 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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://pdbe.org/1s13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s13 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 34:		Line 34:

	==See Also==		==See Also==
-	*[[Heme oxygenase\|Heme oxygenase]]	+	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 41:		Line 41:
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Buldain, G]]		[[Category: Buldain, G]]
	[[Category: Lad, L]]		[[Category: Lad, L]]

OCA at 06:39, 8 March 2018

OCA — Thu, 08 Mar 2018 06:39:10 GMT

←Older revision		Revision as of 06:39, 8 March 2018
Line 1:		Line 1:
		+
	==Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes==		==Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes==
	<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>		<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://pdbe.org/1s13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://pdbe.org/1s13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s13 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s1/1s13_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s1/1s13_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 14:19, 8 February 2016

OCA — Mon, 08 Feb 2016 14:19:09 GMT

←Older revision		Revision as of 14:19, 8 February 2016
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	<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=1s13 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 12:24, 10 September 2015

OCA — Thu, 10 Sep 2015 12:24:10 GMT

←Older revision		Revision as of 12:24, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>		<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S13 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S13 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://pdbe.org/1s13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		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 1s13" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Buldain, G]]		[[Category: Buldain, G]]
	[[Category: Lad, L]]		[[Category: Lad, L]]

OCA at 07:43, 6 January 2015

OCA — Tue, 06 Jan 2015 07:43:10 GMT

←Older revision		Revision as of 07:43, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S13 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S13 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 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=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>		[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
Line 39:		Line 39:
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Buldain, G.]]	+	[[Category: Buldain, G]]
-	[[Category: Lad, L.]]	+	[[Category: Lad, L]]
-	[[Category: Montellano, P R.Ortiz de.]]	+	[[Category: Montellano, P R.Ortiz de]]
-	[[Category: Niemevz, F.]]	+	[[Category: Niemevz, F]]
-	[[Category: Poulos, T L.]]	+	[[Category: Poulos, T L]]
-	[[Category: Wang, J.]]	+	[[Category: Wang, J]]
	[[Category: Heme degradation]]		[[Category: Heme degradation]]
	[[Category: Heme oxygenase-1]]		[[Category: Heme oxygenase-1]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 15:23, 29 September 2014

OCA — Mon, 29 Sep 2014 15:23:20 GMT

←Older revision		Revision as of 15:23, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1s13\| PDB=1s13 \| SCENE= }}~~	+	==Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes==
-	===Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes===	+	<StructureSection load='1s13' size='340' side='right' caption='[[1s13]], [[Resolution\|resolution]] 2.29Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15297453}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1s13]] is a 2 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=1S13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S13 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FH:2-PHENYLHEME'>2FH</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMOX1 or HO1 or HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s13 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s13 RCSB], [http://www.ebi.ac.uk/pdbsum/1s13 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] 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 ==
		+	[[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/s1/1s13_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 ==
		+	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron. Previous work indicated that electrophilic addition of the terminal oxygen of the ferric hydroperoxo complex to the alpha-meso-carbon gives 5-hydroxyheme. Earlier efforts to block this reaction with a 5-methyl substituent failed, as the reaction still gave biliverdin IXalpha. Surprisingly, a 15-methyl substituent caused exclusive cleavage at the gamma-meso-rather than at the normal, unsubstituted alpha-meso-carbon. No CO was formed in these reactions, but the fragment cleaved from the porphyrin eluded identification. We report here that hHO-1 cleaves 5-phenylheme to biliverdin IXalpha and oxidizes 15-phenylheme at the alpha-meso position to give 10-phenylbiliverdin IXalpha. The fragment extruded in the oxidation of 5-phenylheme is benzoic acid, one oxygen of which comes from O2 and the other from water. The 2.29- and 2.11-A crystal structures of the hHO-1 complexes with 1- and 15-phenylheme, respectively, show clear electron density for both the 5- and 15-phenyl rings in both molecules of the asymmetric unit. The overall structure of 15-phenylheme-hHO-1 is similar to that of heme-hHO-1 except for small changes in distal residues 141-150 and in the proximal Lys18 and Lys22. In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon. The results provide independent support for an electrophilic oxidation mechanism and support a role for stereochemical control of the reaction regiospecificity.

-	~~==Disease==~~	+	Human heme oxygenase oxidation of 5- and 15-phenylhemes.,Wang J, Niemevz F, Lad L, Huang L, Alvarez DE, Buldain G, Poulos TL, de Montellano PR J Biol Chem. 2004 Oct 8;279(41):42593-604. Epub 2004 Aug 5. PMID:15297453<ref>PMID:15297453</ref>
-	~~[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of~~ heme oxygenase ~~1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]~~. ~~A disease characterized by impaired stress hematopoiesis~~, ~~resulting in marked erythrocyte fragmentation and intravascular hemolysis~~, ~~coagulation abnormalities~~, ~~endothelial damage~~, ~~and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia~~, ~~asplenia~~, ~~nephritis~~, ~~generalized erythematous rash~~, ~~growth retardation and hepatomegaly~~.<ref>PMID:~~9884342~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] 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~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1s13]] is a 2 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=1S13 OCA].~~	+

	==See Also==		==See Also==
	*[[Heme oxygenase\|Heme oxygenase]]		*[[Heme oxygenase\|Heme oxygenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:015297453</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 17:06, 24 March 2013

OCA — Sun, 24 Mar 2013 17:06:04 GMT

←Older revision		Revision as of 17:06, 24 March 2013
Line 1:		Line 1:
-	[[Image:1s13.png\|left\|200px]]
-
	{{STRUCTURE_1s13\| PDB=1s13 \| SCENE= }}		{{STRUCTURE_1s13\| PDB=1s13 \| SCENE= }}
-
	===Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes===		===Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes===
		+	{{ABSTRACT_PUBMED_15297453}}

-	~~{{ABSTRACT_PUBMED_15297453}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] 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.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:015297453</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015297453</ref><references group="xtra"/><references/>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 10:26, 20 October 2012

OCA — Sat, 20 Oct 2012 10:26:14 GMT

←Older revision		Revision as of 10:26, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1s13]] is a 2 chain structure ~~of [[Heme oxygenase]]~~ 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=1S13 OCA].	+	[[1s13]] is a 2 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=1S13 OCA].

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

OCA: Protected "1s13" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 02:07:12 GMT

Protected "1s13" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:07, 26 July 2012