2q3j - Revision history

OCA at 11:17, 30 August 2023

OCA — Wed, 30 Aug 2023 11:17:20 GMT

←Older revision		Revision as of 11:17, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='2q3j' size='340' side='right'caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='2q3j' size='340' side='right'caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"vibrio_subtilis"_ehrenberg_1835 "vibrio~~ subtilis~~" ehrenberg 1835~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=H02:N~~-~~METHYL+PROTOPORPHYRIN+IX+2~~,~~4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.39Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[2q2n\|2q2n]], [[2q2o\|2q2o]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>hemH, hemF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1423~~ "~~Vibrio subtilis~~" ~~Ehrenberg 1835])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [https://pdbe.org/2q3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [https://www.ebi.ac.uk/pdbsum/2q3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [https://pdbe.org/2q3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [https://www.ebi.ac.uk/pdbsum/2q3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~HEMH_BACSU HEMH_BACSU]~~] Catalyzes the ~~ferrous~~ insertion into protoporphyrin IX.	+	[https://www.uniprot.org/uniprot/CPFC_BACSU CPFC_BACSU] Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).<ref>PMID:12761666</ref> <ref>PMID:1459957</ref> <ref>PMID:16140324</ref> <ref>PMID:21052751</ref> <ref>PMID:25646457</ref> <ref>PMID:25826316</ref> <ref>PMID:25908396</ref> <ref>PMID:8119288</ref>
	== 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: ~~Vibrio~~ subtilis ~~ehrenberg 1835]]~~	+	[[Category: Bacillus subtilis]]
-	~~[[Category: Ferrochelatase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Al-Karadaghi, S]]	+	[[Category: Al-Karadaghi S]]
-	[[Category: Karlberg, T]]	+	[[Category: Karlberg T]]
-	[[Category: Thorvaldsen~~, O H]]~~	+	[[Category: Thorvaldsen OH]]
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: N-memp]]~~	+
-	~~[[Category: N-methyl mesoporphyrin ix]]~~	+
-	~~[[Category: Pi-helix]]~~	+
-	~~[[Category: Rossmann fold~~]]	+

OCA at 08:06, 25 June 2021

OCA — Fri, 25 Jun 2021 08:06:40 GMT

←Older revision		Revision as of 08:06, 25 June 2021
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	==Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin==		==Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin==
-	<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>	+	<StructureSection load='2q3j' size='340' side='right'caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2q2n\|2q2n]], [[2q2o\|2q2o]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [~~http~~://pdbe.org/2q3j PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2q3j PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [https://pdbe.org/2q3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [https://www.ebi.ac.uk/pdbsum/2q3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HEMH_BACSU HEMH_BACSU]] Catalyzes the ferrous insertion into protoporphyrin IX.	+	[[https://www.uniprot.org/uniprot/HEMH_BACSU HEMH_BACSU]] 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]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Ferrochelatase\|Ferrochelatase]]	+	*[[Ferrochelatase 3D structures\|Ferrochelatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Vibrio subtilis ehrenberg 1835]]		[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
		+	[[Category: Large Structures]]
	[[Category: Al-Karadaghi, S]]		[[Category: Al-Karadaghi, S]]
	[[Category: Karlberg, T]]		[[Category: Karlberg, T]]

OCA at 05:35, 8 March 2018

OCA — Thu, 08 Mar 2018 05:35:15 GMT

←Older revision		Revision as of 05:35, 8 March 2018
Line 1:		Line 1:
		+
	==Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin==		==Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin==
	<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"~~bacillus_globigii~~"~~_migula_1900~~ "~~bacillus globigii~~" ~~migula 1900~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "~~Bacillus globigii~~" ~~Migula 1900~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://pdbe.org/2q3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://pdbe.org/2q3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q3/2q3j_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q3/2q3j_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>
	</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=2q3j ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus globigii migula 1900~~]]	+	[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Al-Karadaghi, S]]		[[Category: Al-Karadaghi, S]]

OCA at 11:46, 11 September 2015

OCA — Fri, 11 Sep 2015 11:46:53 GMT

←Older revision		Revision as of 11:46, 11 September 2015
Line 7:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://pdbe.org/2q3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	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 2q3j" style="background-color:#fffaf0;"></div>

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

OCA at 16:02, 25 December 2014

OCA — Thu, 25 Dec 2014 16:02:23 GMT

←Older revision		Revision as of 16:02, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HEMH_BACSU HEMH_BACSU]] 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]]
Line 33:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus globigii migula 1900]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Al-Karadaghi, S]]		[[Category: Al-Karadaghi, S]]

OCA at 07:20, 12 November 2014

OCA — Wed, 12 Nov 2014 07:20:49 GMT

←Older revision		Revision as of 07:20, 12 November 2014
Line 2:		Line 2:
	<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum]</span></td></tr>
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus subtilis]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
-	[[Category: Al-Karadaghi, S.]]	+	[[Category: Al-Karadaghi, S]]
-	[[Category: Karlberg, T.]]	+	[[Category: Karlberg, T]]
-	[[Category: Thorvaldsen, O H.]]	+	[[Category: Thorvaldsen, O H]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: N-memp]]		[[Category: N-memp]]

OCA at 14:26, 3 November 2014

OCA — Mon, 03 Nov 2014 14:26:30 GMT

←Older revision		Revision as of 14:26, 3 November 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>		<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j 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=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 43:		Line 43:
	[[Category: N-methyl mesoporphyrin ix]]		[[Category: N-methyl mesoporphyrin ix]]
	[[Category: Pi-helix]]		[[Category: Pi-helix]]
-	[[Category: ~~Rossman~~ fold]]	+	[[Category: Rossmann fold]]

OCA at 19:08, 30 September 2014

OCA — Tue, 30 Sep 2014 19:08:28 GMT

←Older revision		Revision as of 19:08, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2q3j.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin==
		+	<StructureSection load='2q3j' size='340' side='right' caption='[[2q3j]], [[Resolution\|resolution]] 2.39Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q3J FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H02:N-METHYL+PROTOPORPHYRIN+IX+2,4-DISULFONIC+ACID'>H02</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2q2n\|2q2n]], [[2q2o\|2q2o]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2q3j RCSB], [http://www.ebi.ac.uk/pdbsum/2q3j PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q3/2q3j_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 ==
		+	The specific insertion of a divalent metal ion into tetrapyrrole macrocycles is catalyzed by a group of enzymes called chelatases. Distortion of the tetrapyrrole has been proposed to be an important component of the mechanism of metallation. We present the structures of two different inhibitor complexes: (1) N-methylmesoporphyrin (N-MeMP) with the His183Ala variant of Bacillus subtilis ferrochelatase; (2) the wild-type form of the same enzyme with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride (dSDP). Analysis of the structures showed that only one N-MeMP isomer out of the eight possible was bound to the protein and it was different from the isomer that was earlier found to bind to the wild-type enzyme. A comparison of the distortion of this porphyrin with other porphyrin complexes of ferrochelatase and a catalytic antibody with ferrochelatase activity using normal-coordinate structural decomposition reveals that certain types of distortion are predominant in all these complexes. On the other hand, dSDP, which binds closer to the protein surface compared to N-MeMP, does not undergo any distortion upon binding to the protein, underscoring that the position of the porphyrin within the active site pocket is crucial for generating the distortion required for metal insertion. In addition, in contrast to the wild-type enzyme, Cu(2+)-soaking of the His183Ala variant complex did not show any traces of porphyrin metallation. Collectively, these results provide new insights into the role of the active site residues of ferrochelatase in controlling stereospecificity, distortion and metallation.

-	~~{{STRUCTURE_2q3j\| PDB=2q3j \| SCENE= }}~~	+	Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.,Karlberg T, Hansson MD, Yengo RK, Johansson R, Thorvaldsen HO, Ferreira GC, Hansson M, Al-Karadaghi S J Mol Biol. 2008 May 16;378(5):1074-83. Epub 2008 Mar 28. PMID:18423489<ref>PMID:18423489</ref>

-	~~===Crystal structure~~ of the ~~His183Ala variant~~ of ~~Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_18423489}}~~	+	==See Also==
-		+	*[[Ferrochelatase\|Ferrochelatase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~2q3j~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:018423489<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]

OCA: Protected "2q3j" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 19:09:17 GMT

Protected "2q3j" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:09, 7 January 2013

OCA at 19:09, 7 January 2013

OCA — Mon, 07 Jan 2013 19:09:12 GMT

←Older revision		Revision as of 19:09, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2q3j.png\|left\|200px]]		[[Image:2q3j.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2q3j", 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_2q3j\| PDB=2q3j \| SCENE= }}		{{STRUCTURE_2q3j\| PDB=2q3j \| SCENE= }}

	===Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin===		===Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18423489}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18423489 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18423489}}		{{ABSTRACT_PUBMED_18423489}}

	==About this Structure==		==About this Structure==
-	~~2Q3J~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA].	+	[[2q3j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3J OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18423489~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018423489</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
Line 34:		Line 22:
	[[Category: Pi-helix]]		[[Category: Pi-helix]]
	[[Category: Rossman fold]]		[[Category: Rossman fold]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:12:20 2009''