3hco - Revision history

OCA at 09:59, 21 February 2024

OCA — Wed, 21 Feb 2024 09:59:13 GMT

←Older revision		Revision as of 09:59, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3hco' size='340' side='right'caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3hco' size='340' side='right'caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hco]] is a 2 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HCO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH, hemH ([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'>[https://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [https://pdbe.org/3hco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [https://www.ebi.ac.uk/pdbsum/3hco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hco 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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [https://pdbe.org/3hco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [https://www.ebi.ac.uk/pdbsum/3hco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hco ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>	+	[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.	+	[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN] Catalyzes the ferrous insertion into protoporphyrin IX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3hco 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=3hco ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Ferrochelatase (protoheme ferrolyase, E.C. 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Within the past two years, X-ray crystallographic data obtained with human ferrochelatase have clearly shown that significant structural changes occur during catalysis that are predicted to facilitate metal insertion and product release. One unanswered question about ferrochelatase involves defining the mechanism whereby some metals, such as divalent Fe, Co, Ni, and Zn, can be used by the enzyme in vitro to produce the corresponding metalloporphyrins, while other metals, such as divalent Mn, Hg, Cd, or Pb, are inhibitors of the enzyme. Through the use of high-resolution X-ray crystallography along with characterization of metal species via their anomalous diffraction, the identity and position of Hg, Cd, Ni, or Mn in the center of enzyme-bound porphyrin macrocycle were determined. When Pb, Hg, Cd, or Ni was present in the macrocycle, the conserved pi helix was in the extended, partially unwound "product release" state. Interestingly, in the structure of ferrochelatase with Mn-porphyrin bound, the pi helix is not extended or unwound and is in the "substrate-bound" conformation. These findings show that at least in the cases of Mn, Pb, Cd, and Hg, metal "inhibition" of ferrochelatase is not due to the inability of the enzyme to insert the metal into the macrocycle or by binding to a second metal binding site as has been previously proposed. Rather, inhibition occurs after metal insertion and results from poor or diminished product release. Possible explanations for the lack of product release are proposed herein.
-
-	Product release rather than chelation determines metal specificity for ferrochelatase.,Medlock AE, Carter M, Dailey TA, Dailey HA, Lanzilotta WN J Mol Biol. 2009 Oct 23;393(2):308-19. Epub 2009 Aug 22. PMID:19703464<ref>PMID:19703464</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3hco" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ferrochelatase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dailey~~, H A~~]]	+	[[Category: Dailey HA]]
-	[[Category: Lanzilotta~~, W N~~]]	+	[[Category: Lanzilotta WN]]
-	[[Category: Medlock~~, A E]]~~	+	[[Category: Medlock AE]]
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Heme biosynthesis]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Iron-sulfur]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Metal selectivity]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Mitochondrion inner membrane]]~~	+
-	~~[[Category: Porphyrin biosynthesis]]~~	+
-	~~[[Category: Transit peptide~~]]	+

OCA at 08:08, 16 March 2022

OCA — Wed, 16 Mar 2022 08:08:47 GMT

OCA at 08:18, 24 July 2019

OCA — Wed, 24 Jul 2019 08:18:12 GMT

←Older revision		Revision as of 08:18, 24 July 2019
Line 1:		Line 1:

	==Human ferrochelatase with Cd and protoporphyrin IX bound==		==Human ferrochelatase with Cd and protoporphyrin IX bound==
-	<StructureSection load='3hco' size='340' side='right' caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3hco' size='340' side='right'caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCO FirstGlance]. <br>
Line 35:		Line 35:

	==See Also==		==See Also==
-	*[[Ferrochelatase\|Ferrochelatase]]	+	*[[Ferrochelatase 3D structures\|Ferrochelatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 42:		Line 42:
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Dailey, H A]]		[[Category: Dailey, H A]]
	[[Category: Lanzilotta, W N]]		[[Category: Lanzilotta, W N]]

OCA at 08:01, 12 December 2018

OCA — Wed, 12 Dec 2018 08:01:44 GMT

←Older revision		Revision as of 08:01, 12 December 2018
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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/hc/3hco_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/3hco_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 21:38, 5 August 2016

OCA — Fri, 05 Aug 2016 21:38:27 GMT

←Older revision		Revision as of 21:38, 5 August 2016
Line 1:		Line 1:
		+
	==Human ferrochelatase with Cd and protoporphyrin IX bound==		==Human ferrochelatase with Cd and protoporphyrin IX bound==
	<StructureSection load='3hco' size='340' side='right' caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3hco' size='340' side='right' caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH, hemH ([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">FECH, hemH ([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/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [http://www.ebi.ac.uk/pdbsum/3hco 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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [http://pdbe.org/3hco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [http://www.ebi.ac.uk/pdbsum/3hco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hco ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	<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=3hco 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:
	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 3hco" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 41:
	</StructureSection>		</StructureSection>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Dailey, H A]]		[[Category: Dailey, H A]]
	[[Category: Lanzilotta, W N]]		[[Category: Lanzilotta, W N]]

OCA at 17:01, 18 December 2014

OCA — Thu, 18 Dec 2014 17:01:29 GMT

←Older revision		Revision as of 17:01, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3hco~~\| ~~PDB~~=3hco \| ~~SCENE~~= }}	+	==Human ferrochelatase with Cd and protoporphyrin IX bound==
-	===~~Human ferrochelatase~~ with Cd and protoporphyrin IX ~~bound~~===	+	<StructureSection load='3hco' size='340' side='right' caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19703464}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HCO FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH, hemH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [http://www.ebi.ac.uk/pdbsum/3hco PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.
		+	== 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/hc/3hco_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 ==
		+	Ferrochelatase (protoheme ferrolyase, E.C. 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Within the past two years, X-ray crystallographic data obtained with human ferrochelatase have clearly shown that significant structural changes occur during catalysis that are predicted to facilitate metal insertion and product release. One unanswered question about ferrochelatase involves defining the mechanism whereby some metals, such as divalent Fe, Co, Ni, and Zn, can be used by the enzyme in vitro to produce the corresponding metalloporphyrins, while other metals, such as divalent Mn, Hg, Cd, or Pb, are inhibitors of the enzyme. Through the use of high-resolution X-ray crystallography along with characterization of metal species via their anomalous diffraction, the identity and position of Hg, Cd, Ni, or Mn in the center of enzyme-bound porphyrin macrocycle were determined. When Pb, Hg, Cd, or Ni was present in the macrocycle, the conserved pi helix was in the extended, partially unwound "product release" state. Interestingly, in the structure of ferrochelatase with Mn-porphyrin bound, the pi helix is not extended or unwound and is in the "substrate-bound" conformation. These findings show that at least in the cases of Mn, Pb, Cd, and Hg, metal "inhibition" of ferrochelatase is not due to the inability of the enzyme to insert the metal into the macrocycle or by binding to a second metal binding site as has been previously proposed. Rather, inhibition occurs after metal insertion and results from poor or diminished product release. Possible explanations for the lack of product release are proposed herein.

-	~~==Disease==~~	+	Product release rather than chelation determines metal specificity for ferrochelatase.,Medlock AE, Carter M, Dailey TA, Dailey HA, Lanzilotta WN J Mol Biol. 2009 Oct 23;393(2):308-19. Epub 2009 Aug 22. PMID:19703464<ref>PMID:19703464</ref>
-	~~[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]~~. ~~Porphyrias are inherited defects in the biosynthesis of heme~~, ~~resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic~~, ~~depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes~~, ~~plasma~~, ~~liver and feces~~, ~~and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals~~.~~<ref>PMID~~:~~1755842</ref><ref>~~PMID:1376018</ref><ref>PMID:7910885</ref><ref>PMID:8757534</ref><ref>PMID:9585598</ref><ref>PMID:9740232</ref><ref>PMID:10942404</ref><ref>PMID:11375302</ref><ref>PMID:12063482</ref><ref>PMID:12601550</ref><ref>PMID:15286165</ref><ref>PMID:~~17196862~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[3hco]] 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=3HCO OCA].~~	+

	==See Also==		==See Also==
	*[[Ferrochelatase\|Ferrochelatase]]		*[[Ferrochelatase\|Ferrochelatase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019703464</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Dailey, H A.]]	+	[[Category: Dailey, H A]]
-	[[Category: Lanzilotta, W N.]]	+	[[Category: Lanzilotta, W N]]
-	[[Category: Medlock, A E.]]	+	[[Category: Medlock, A E]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
-	[[Category: Ferrochelatase]]
	[[Category: Heme biosynthesis]]		[[Category: Heme biosynthesis]]
	[[Category: Iron]]		[[Category: Iron]]

OCA at 05:53, 25 March 2013

OCA — Mon, 25 Mar 2013 05:53:53 GMT

←Older revision		Revision as of 05:53, 25 March 2013
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-	[[Image:3hco.png\|left\|200px]]
-
	{{STRUCTURE_3hco\| PDB=3hco \| SCENE= }}		{{STRUCTURE_3hco\| PDB=3hco \| SCENE= }}
-
	===Human ferrochelatase with Cd and protoporphyrin IX bound===		===Human ferrochelatase with Cd and protoporphyrin IX bound===
		+	{{ABSTRACT_PUBMED_19703464}}

-	~~{{ABSTRACT_PUBMED_19703464}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref><ref>PMID:1376018</ref><ref>PMID:7910885</ref><ref>PMID:8757534</ref><ref>PMID:9585598</ref><ref>PMID:9740232</ref><ref>PMID:10942404</ref><ref>PMID:11375302</ref><ref>PMID:12063482</ref><ref>PMID:12601550</ref><ref>PMID:15286165</ref><ref>PMID:17196862</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019703464</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019703464</ref><references group="xtra"/><references/>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

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

OCA — Wed, 06 Mar 2013 14:40:46 GMT

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

←Older revision

Revision as of 14:40, 6 March 2013

OCA at 14:40, 6 March 2013

OCA — Wed, 06 Mar 2013 14:40:44 GMT

←Older revision		Revision as of 14:40, 6 March 2013
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-	{{Seed}}
	[[Image:3hco.png\|left\|200px]]		[[Image:3hco.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3hco", 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_3hco\| PDB=3hco \| SCENE= }}		{{STRUCTURE_3hco\| PDB=3hco \| SCENE= }}

	===Human ferrochelatase with Cd and protoporphyrin IX bound===		===Human ferrochelatase with Cd and protoporphyrin IX bound===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19703464}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19703464 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19703464}}		{{ABSTRACT_PUBMED_19703464}}

	==About this Structure==		==About this Structure==
-	~~3HCO~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCO OCA].	+	[[3hco]] 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=3HCO OCA].
		+
		+	==See Also==
		+	*[[Ferrochelatase\|Ferrochelatase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19703464~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019703464</ref><references group="xtra"/>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 29:		Line 20:
	[[Category: Lanzilotta, W N.]]		[[Category: Lanzilotta, W N.]]
	[[Category: Medlock, A E.]]		[[Category: Medlock, A E.]]
-	[[Category: 2fe-2]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
Line 41:		Line 31:
	[[Category: Mitochondrion]]		[[Category: Mitochondrion]]
	[[Category: Mitochondrion inner membrane]]		[[Category: Mitochondrion inner membrane]]
-	[[Category: Polymorphism]]
	[[Category: Porphyrin biosynthesis]]		[[Category: Porphyrin biosynthesis]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 28 15:16:41 2010''

OCA at 13:16, 28 January 2010

OCA — Thu, 28 Jan 2010 13:16:42 GMT

←Older revision		Revision as of 13:16, 28 January 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3hco.~~jpg~~\|left\|200px]]	+	[[Image:3hco.png\|left\|200px]]

	<!--		<!--
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	3HCO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCO OCA].	+	3HCO is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCO OCA].

	==Reference==		==Reference==
Line 45:		Line 45:
	[[Category: Transit peptide]]		[[Category: Transit peptide]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Nov 11 22~~:25:~~51 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 28 15:16:41 2010''

←Older revision		Revision as of 08:08, 16 March 2022
Line 3:		Line 3:
	<StructureSection load='3hco' size='340' side='right'caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3hco' size='340' side='right'caption='[[3hco]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hco]] 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hco]] is a 2 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=3HCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HCO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hcn\|3hcn]], [[3hcp\|3hcp]], [[3hcr\|3hcr]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH, hemH ([~~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">FECH, hemH ([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/Ferrochelatase Ferrochelatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [~~http~~://pdbe.org/3hco PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hco PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hco 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=3hco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hco OCA], [https://pdbe.org/3hco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hco RCSB], [https://www.ebi.ac.uk/pdbsum/3hco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hco ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[~~http~~://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>	+	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.	+	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]