5req - Revision history

OCA at 12:29, 13 August 2026

2026-08-13T12:29:21Z

← Older revision		Revision as of 12:29, 13 August 2026
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	<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5REQ FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.2Å</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]] 2.2Å</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat">~~<scene name='pdbligand=B12:COBALAMIN'>B12</scene>,~~ <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [https://pdbe.org/5req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [https://www.ebi.ac.uk/pdbsum/5req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5req 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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [https://pdbe.org/5req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [https://www.ebi.ac.uk/pdbsum/5req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5req ProSAT]</span></td></tr>
	</table>		</table>
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/5req_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/5req_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 18:05, 20 September 2023

2023-09-20T18:05:21Z

← Older revision		Revision as of 18:05, 20 September 2023
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	<StructureSection load='5req' size='340' side='right'caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5req' size='340' side='right'caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"propionibacterium_shermanii"_van_niel_1928 "propionibacterium~~ shermanii~~" van niel 1928~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5REQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</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]] 2.2Å</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928]), MUTA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [https://pdbe.org/5req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [https://www.ebi.ac.uk/pdbsum/5req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5req 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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [https://pdbe.org/5req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [https://www.ebi.ac.uk/pdbsum/5req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5req ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR~~]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[https://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]~~] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.		[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== 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: Propionibacterium shermanii van niel 1928]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Methylmalonyl-CoA mutase~~]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	[[Category: Evans~~, P R~~]]		[[Category: Evans PR]]
	[[Category: Thomae~~, N H]]~~		[[Category: Thomae NH]]
	~~[[Category: Intramolecular transferase]]~~
	~~[[Category: Isomerase]]~~
	~~[[Category: Mutase~~]]

OCA at 15:51, 3 November 2021

2021-11-03T15:51:48Z

← Older revision		Revision as of 15:51, 3 November 2021
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	==Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex==		==Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex==
	<StructureSection load='5req' size='340' side='right' caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5req' size='340' side='right'caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5REQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928]), MUTA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928]), MUTA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [~~http~~://pdbe.org/5req PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5req PDBsum]</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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [https://pdbe.org/5req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [https://www.ebi.ac.uk/pdbsum/5req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5req ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[~~http~~://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.		[[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[https://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/5req_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/5req_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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	</StructureSection>		</StructureSection>
	[[Category: Propionibacterium shermanii van niel 1928]]		[[Category: Propionibacterium shermanii van niel 1928]]
			[[Category: Large Structures]]
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Evans, P R]]		[[Category: Evans, P R]]

OCA at 08:29, 9 February 2016

2016-02-09T08:29:00Z

← Older revision		Revision as of 08:29, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='5req' size='340' side='right' caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5req' size='340' side='right' caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp.~~ shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5REQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium ~~freudenreichii subsp.~~ shermanii]), MUTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium ~~freudenreichii subsp.~~ shermanii])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928]), MUTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [http://www.ebi.ac.uk/pdbsum/5req 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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [http://pdbe.org/5req PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [http://www.ebi.ac.uk/pdbsum/5req PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5req ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	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 5req" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	~~[[Category: Propionibacterium freudenreichii subsp. shermanii]]~~
	[[Category: Evans, P R]]		[[Category: Evans, P R]]
	[[Category: Thomae, N H]]		[[Category: Thomae, N H]]

OCA at 05:43, 25 December 2014

2014-12-25T05:43:36Z

← Older revision		Revision as of 05:43, 25 December 2014
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	<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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [http://www.ebi.ac.uk/pdbsum/5req 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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [http://www.ebi.ac.uk/pdbsum/5req PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[http://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:58, 10 December 2014

2014-12-10T16:58:56Z

← Older revision		Revision as of 16:58, 10 December 2014
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	[[Image:~~5req~~.~~png~~\|~~left~~\|~~200px~~]]		==Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex==
			<StructureSection load='5req' size='340' side='right' caption='[[5req]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[5req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5REQ FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCD:METHYLMALONYL(CARBADETHIA)-COENZYME+A'>MCD</scene>, <scene name='pdbligand=SCD:SUCCINYL(CARBADETHIA)-COENZYME+A'>SCD</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]), MUTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=5req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5req RCSB], [http://www.ebi.ac.uk/pdbsum/5req 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/re/5req_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 adenosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the reversible rearrangement of methylmalonyl-CoA into succinyl-CoA by a free-radical mechanism. The recently solved X-ray crystal structure of methylmalonyl-CoA mutase from Propionibacterium shermanii has shown that tyrosine 89 is an active-site residue involved in substrate binding. The role of tyrosine 89, a conserved residue among methylmalonyl-CoA mutases, has been investigated by using site-directed mutagenesis to replace this residue with phenylalanine. The crystal structure of the Tyr89Phe mutant was determined to 2.2 A resolution and was found to be essentially superimposable on that of wild-type. Mutant and wild-type enzyme have very similar KM values, but kcat for the Tyr89Phe mutant is 580-fold lower than for wild-type. The rate of release of tritium from 5'-[3H]adenosylcobalamin during the enzymatic reaction and its rate of appearance in substrate and product were measured. The tritium released was found to partition unequally between methylmalonyl-CoA and succinyl-CoA, in a ratio of 40:60 when the reaction was initiated by addition of methylmalonyl-CoA and in a ratio of 10:90 when the reaction was initiated by addition of succinyl-CoA. The overall release of tritium was four times faster when succinyl-CoA was used as substrate. The tritium isotope effect on the enzyme catalyzed hydrogen transfer, measured with methylmalonyl-CoA as a substrate, was kH/kT = 30, which is within the expected range for a full primary kinetic tritium isotope effect. The different partitioning of tritium, dependent upon which substrate was used, and the normal value for the kinetic tritium isotope effect contrast markedly with the behavior of wild-type mutase. It appears that the loss of a single interaction involving the hydroxyl group of tyrosine 89 both affects the stability of radical intermediates and decreases the rate of interconversion of the substrate- and product-derived radicals.

	~~{{STRUCTURE_5req\| PDB=5req \| SCENE= }}~~		Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.,Thoma NH, Meier TW, Evans PR, Leadlay PF Biochemistry. 1998 Oct 13;37(41):14386-93. PMID:9772164<ref>PMID:9772164</ref>

	~~===Methylmalonyl-COA MUTASE~~, ~~Y89F Mutant, substrate complex===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_9772164}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[5req]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Propionibacterium_freudenreichii_subsp~~.~~_shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:009772164<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	[[Category: Evans, P R.]]		[[Category: Evans, P R]]
	[[Category: Thomae, N H.]]		[[Category: Thomae, N H]]
	[[Category: Intramolecular transferase]]		[[Category: Intramolecular transferase]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Mutase]]		[[Category: Mutase]]

OCA: Protected "5req" [edit=sysop:move=sysop]

2012-10-24T06:25:04Z

Protected "5req" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:25, 24 October 2012
(No difference)

OCA at 06:25, 24 October 2012

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	~~{{Seed}}~~
	[[Image:5req.png\|left\|200px]]		[[Image:5req.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_5req", 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_5req\| PDB=5req \| SCENE= }}		{{STRUCTURE_5req\| PDB=5req \| SCENE= }}

	===Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex===		===Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_9772164}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 9772164 is the PubMed ID number.~~
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	{{ABSTRACT_PUBMED_9772164}}		{{ABSTRACT_PUBMED_9772164}}

	==About this Structure==		==About this Structure==
	~~5REQ~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].		[[5req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~9772164~~</ref><references group="xtra"/>		<ref group="xtra">PMID:009772164</ref><references group="xtra"/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
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	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Mutase]]		[[Category: Mutase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:01:04 2010''~~

OCA at 06:01, 20 May 2010

2010-05-20T06:01:04Z

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	{{STRUCTURE_5req\| PDB=5req \| SCENE= }}		{{STRUCTURE_5req\| PDB=5req \| SCENE= }}

	===~~METHYLMALONYL~~-COA MUTASE, Y89F ~~MUTANT~~, ~~SUBSTRATE COMPLEX~~===		===Methylmalonyl-COA MUTASE, Y89F Mutant, substrate complex===


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	==About this Structure==		==About this Structure==
	5REQ is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].		5REQ is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].

	==Reference==		==Reference==
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	[[Category: Mutase]]		[[Category: Mutase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Feb 17 08~~:22:~~08 2009~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:01:04 2010''

OCA at 06:22, 17 February 2009

2009-02-17T06:22:10Z

← Older revision		Revision as of 06:22, 17 February 2009
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	==About this Structure==		==About this Structure==
	5REQ is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].		5REQ is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5REQ OCA].

	==Reference==		==Reference==
	~~Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase., Thoma NH, Meier TW, Evans PR, Leadlay PF, Biochemistry. 1998 Oct 13;37(41):14386-93.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9772164 9772164]~~		<ref group="xtra">PMID:9772164</ref><references group="xtra"/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	~~[[Category: Protein complex]]~~
	[[Category: Evans, P R.]]		[[Category: Evans, P R.]]
	[[Category: Thomae, N H.]]		[[Category: Thomae, N H.]]
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	[[Category: Mutase]]		[[Category: Mutase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jul 3 14~~:10:~~13 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:22:08 2009''