1ni6 - Revision history

OCA at 09:20, 16 August 2023

OCA — Wed, 16 Aug 2023 09:20:32 GMT

←Older revision		Revision as of 09:20, 16 August 2023
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	<StructureSection load='1ni6' size='340' side='right'caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ni6' size='340' side='right'caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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]] 2.1Å</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=9606 HUMAN])</td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene></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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [https://pdbe.org/1ni6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ni6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni6 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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [https://pdbe.org/1ni6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ni6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni6 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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>	+	[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 ==
-	[[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.	+	[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: Friedman, J]]	+	[[Category: Friedman J]]
-	[[Category: Lad, L]]	+	[[Category: Lad L]]
-	[[Category: Li, H]]	+	[[Category: Li H]]
-	[[Category: ~~Montellano, P R.~~Ortiz de]]	+	[[Category: Ortiz de Montellano PR]]
-	[[Category: Poulos~~, T L~~]]	+	[[Category: Poulos TL]]
-	[[Category: Schuller~~, D J~~]]	+	[[Category: Schuller DJ]]
-	[[Category: Shimizu, H]]	+	[[Category: Shimizu H]]
-	~~[[Category: Heme degradation]]~~	+
-	~~[[Category: Heme oxygenase-1]]~~	+
-	~~[[Category: Oxygen storage-transport complex~~]]	+

OCA at 07:03, 25 August 2021

OCA — Wed, 25 Aug 2021 07:03:04 GMT

OCA at 09:13, 30 October 2019

OCA — Wed, 30 Oct 2019 09:13:47 GMT

←Older revision		Revision as of 09:13, 30 October 2019
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	==Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1==		==Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1==
-	<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1ni6' size='340' side='right'caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ni/1ni6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ni/1ni6_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>
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	</div>		</div>
	<div class="pdbe-citations 1ni6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ni6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 41:
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Friedman, J]]		[[Category: Friedman, J]]
	[[Category: Lad, L]]		[[Category: Lad, L]]

OCA at 10:07, 25 October 2017

OCA — Wed, 25 Oct 2017 10:07:14 GMT

←Older revision		Revision as of 10:07, 25 October 2017
Line 1:		Line 1:
		+
	==Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1==		==Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1==
	<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
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	<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=9606 HUMAN])</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=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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://pdbe.org/1ni6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://pdbe.org/1ni6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni6 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<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=1ni6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 1ni6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ni6" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Heme oxygenase\|Heme oxygenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:23, 11 September 2015

OCA — Fri, 11 Sep 2015 15:23:59 GMT

←Older revision		Revision as of 15:23, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></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=9606 ~~Homo sapiens~~])</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=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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://pdbe.org/1ni6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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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 1ni6" 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: Friedman, J]]		[[Category: Friedman, J]]
	[[Category: Lad, L]]		[[Category: Lad, L]]

OCA at 15:52, 5 January 2015

OCA — Mon, 05 Jan 2015 15:52:08 GMT

←Older revision		Revision as of 15:52, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></td></tr>
-	<tr><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=9606 Homo sapiens])</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=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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 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: Friedman, J.]]	+	[[Category: Friedman, J]]
-	[[Category: Lad, L.]]	+	[[Category: Lad, L]]
-	[[Category: Li, H.]]	+	[[Category: Li, H]]
-	[[Category: Montellano, P R.Ortiz de.]]	+	[[Category: Montellano, P R.Ortiz de]]
-	[[Category: Poulos, T L.]]	+	[[Category: Poulos, T L]]
-	[[Category: Schuller, D J.]]	+	[[Category: Schuller, D J]]
-	[[Category: Shimizu, H.]]	+	[[Category: Shimizu, H]]
	[[Category: Heme degradation]]		[[Category: Heme degradation]]
	[[Category: Heme oxygenase-1]]		[[Category: Heme oxygenase-1]]
	[[Category: Oxygen storage-transport complex]]		[[Category: Oxygen storage-transport complex]]

OCA at 17:02, 29 September 2014

OCA — Mon, 29 Sep 2014 17:02:17 GMT

←Older revision		Revision as of 17:02, 29 September 2014
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-	~~{{STRUCTURE_1ni6\| PDB=1ni6 \| SCENE= }}~~	+	==Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1==
-	===Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1===	+	<StructureSection load='1ni6' size='340' side='right' caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12500973}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene><br>
		+	<tr><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=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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ni6 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/ni/1ni6_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 degradation of heme to biliverdin. The crystal structure of human HO-1 in complex with heme reveals a novel helical structure with conserved glycines in the distal helix, providing flexibility to accommodate substrate binding and product release (Schuller, D. J., Wilks, A., Ortiz de Montellano, P. R., and Poulos, T. L. (1999) Nat. Struct. Biol. 6, 860-867). To structurally understand the HO catalytic pathway in more detail, we have determined the crystal structure of human apo-HO-1 at 2.1 A and a higher resolution structure of human HO-1 in complex with heme at 1.5 A. Although the 1.5-A heme.HO-1 model confirms our initial analysis based on the 2.08-A model, the higher resolution structure has revealed important new details such as a solvent H-bonded network in the active site that may be important for catalysis. Because of the absence of the heme, the distal and proximal helices that bracket the heme plane in the holo structure move farther apart in the apo structure, thus increasing the size of the active-site pocket. Nevertheless, the relative positioning and conformation of critical catalytic residues remain unchanged in the apo structure compared with the holo structure, but an important solvent H-bonded network is missing in the apoenzyme. It thus appears that the binding of heme and a tightening of the structure around the heme stabilize the solvent H-bonded network required for proper catalysis.

-	~~==Disease==~~	+	Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1.,Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano PR, Poulos TL J Biol Chem. 2003 Mar 7;278(10):7834-43. Epub 2002 Dec 24. PMID:12500973<ref>PMID:12500973</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==~~	+
-	~~[[1ni6]] 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=1NI6 OCA].~~	+

	==See Also==		==See Also==
	*[[Heme oxygenase\|Heme oxygenase]]		*[[Heme oxygenase\|Heme oxygenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012500973</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 21:05, 24 March 2013

OCA — Sun, 24 Mar 2013 21:05:08 GMT

←Older revision		Revision as of 21:05, 24 March 2013
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-	[[Image:1ni6.png\|left\|200px]]
-
	{{STRUCTURE_1ni6\| PDB=1ni6 \| SCENE= }}		{{STRUCTURE_1ni6\| PDB=1ni6 \| SCENE= }}
-
	===Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1===		===Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1===
		+	{{ABSTRACT_PUBMED_12500973}}

-	~~{{ABSTRACT_PUBMED_12500973}}~~	+	==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:012500973</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012500973</ref><references group="xtra"/><references/>
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 19:54, 20 October 2012

OCA — Sat, 20 Oct 2012 19:54:50 GMT

←Older revision		Revision as of 19:54, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[1ni6]] is a 4 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=1NI6 OCA].	+	[[1ni6]] 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=1NI6 OCA].

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

OCA: Protected "1ni6" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 08:52:27 GMT

Protected "1ni6" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:52, 27 July 2012

←Older revision		Revision as of 07:03, 25 August 2021
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	<StructureSection load='1ni6' size='340' side='right'caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ni6' size='340' side='right'caption='[[1ni6]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ni6]] 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=1NI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NI6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=~~TRE~~:~~TREHALOSE~~'>~~TRE~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></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=9606 HUMAN])</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=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'>[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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [~~http~~://pdbe.org/1ni6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ni6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni6 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=1ni6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni6 OCA], [https://pdbe.org/1ni6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ni6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ni6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ni6 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]]