1dcz - Revision history

OCA at 08:23, 22 May 2024

2024-05-22T08:23:42Z

←Older revision		Revision as of 08:23, 22 May 2024
Line 19:		Line 19:
	</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=1dcz 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=1dcz ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Transcarboxylase (TC) from Propionibacterium shermanii, a biotin-dependent enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and oxalacetate. Within the multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier and also binds the other two subunits to assist in the overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89. The three-dimensional solution structure of the full-length holo-1.3S subunit of TC has been solved by multidimensional heteronuclear NMR spectroscopy. The C-terminal half of the protein (51-123) is folded into a compact all-beta-domain comprising of two four-stranded antiparallel beta-sheets connected by short loops and turns. The fold exhibits a high 2-fold internal symmetry and is similar to that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the intact enzyme, appear to be disordered in the isolated 1.3S subunit. The molecular surface of the folded domain has two distinct surfaces: one side is highly charged, while the other comprises mainly hydrophobic, highly conserved residues.
		+
		+	High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.,Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200<ref>PMID:10704200</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1dcz" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:49, 20 March 2024

2024-03-20T09:49:31Z

←Older revision		Revision as of 09:49, 20 March 2024
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	==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==		==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==
-	<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"propionibacterium_shermanii"_van_niel_1928 "propionibacterium~~ shermanii~~" van niel 1928~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1dd2\|1dd2]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [https://pdbe.org/1dcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [https://www.ebi.ac.uk/pdbsum/1dcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [https://pdbe.org/1dcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [https://www.ebi.ac.uk/pdbsum/1dcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.	+	[https://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 19:
	</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=1dcz 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=1dcz ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Transcarboxylase (TC) from Propionibacterium shermanii, a biotin-dependent enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and oxalacetate. Within the multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier and also binds the other two subunits to assist in the overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89. The three-dimensional solution structure of the full-length holo-1.3S subunit of TC has been solved by multidimensional heteronuclear NMR spectroscopy. The C-terminal half of the protein (51-123) is folded into a compact all-beta-domain comprising of two four-stranded antiparallel beta-sheets connected by short loops and turns. The fold exhibits a high 2-fold internal symmetry and is similar to that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the intact enzyme, appear to be disordered in the isolated 1.3S subunit. The molecular surface of the folded domain has two distinct surfaces: one side is highly charged, while the other comprises mainly hydrophobic, highly conserved residues.
-
-	High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.,Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200<ref>PMID:10704200</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dcz" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Methylmalonyl-CoA carboxytransferase~~]]	+	[[Category: Propionibacterium freudenreichii subsp. shermanii]]
-	[[Category: Carey~~, P R~~]]	+	[[Category: Carey PR]]
-	[[Category: Reddy~~, D V~~]]	+	[[Category: Reddy DV]]
-	[[Category: Shenoy~~, B C~~]]	+	[[Category: Shenoy BC]]
-	[[Category: Sonnichsen~~, F D]]~~	+	[[Category: Sonnichsen FD]]
-	~~[[Category: Antiparallel beta sheet]]~~	+
-	~~[[Category: Biocytin]]~~	+
-	~~[[Category: Hammerhead]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:36, 16 February 2022

2022-02-16T10:36:49Z

←Older revision		Revision as of 10:36, 16 February 2022
Line 3:		Line 3:
	<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dd2\|1dd2]]</div></td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dd2\|1dd2]]</div></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_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Methylmalonyl-CoA carboxytransferase]]		[[Category: Methylmalonyl-CoA carboxytransferase]]

OCA at 18:24, 10 March 2021

2021-03-10T18:24:54Z

←Older revision		Revision as of 18:24, 10 March 2021
Line 3:		Line 3:
	<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dd2\|1dd2]]</div></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_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [~~http~~://pdbe.org/1dcz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dcz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [https://pdbe.org/1dcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [https://www.ebi.ac.uk/pdbsum/1dcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.	+	[[https://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 23:31, 5 June 2019

2019-06-05T23:31:29Z

←Older revision		Revision as of 23:31, 5 June 2019
Line 1:		Line 1:

	==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==		==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==
-	<StructureSection load='1dcz' size='340' side='right' caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1dcz' size='340' side='right'caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcz_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcz_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>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Methylmalonyl-CoA carboxytransferase]]		[[Category: Methylmalonyl-CoA carboxytransferase]]
	[[Category: Carey, P R]]		[[Category: Carey, P R]]

OCA at 04:06, 30 August 2017

2017-08-30T04:06:16Z

←Older revision		Revision as of 04:06, 30 August 2017
Line 1:		Line 1:
		+
	==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==		==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==
	<StructureSection load='1dcz' size='340' side='right' caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1dcz' size='340' side='right' caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</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_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://pdbe.org/1dcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://pdbe.org/1dcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<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=1dcz ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Methylmalonyl-CoA carboxytransferase]]		[[Category: Methylmalonyl-CoA carboxytransferase]]
	[[Category: Carey, P R]]		[[Category: Carey, P R]]

OCA at 00:26, 12 September 2015

2015-09-12T00:26:31Z

←Older revision		Revision as of 00:26, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='1dcz' size='340' side='right' caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1dcz' size='340' side='right' caption='[[1dcz]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp.~~ shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</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_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://pdbe.org/1dcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1dcz" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Methylmalonyl-CoA carboxytransferase]]		[[Category: Methylmalonyl-CoA carboxytransferase]]
-	[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	[[Category: Carey, P R]]		[[Category: Carey, P R]]
	[[Category: Reddy, D V]]		[[Category: Reddy, D V]]

OCA at 21:25, 25 December 2014

2014-12-25T21:25:06Z

←Older revision		Revision as of 21:25, 25 December 2014
Line 7:		Line 7:
	<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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:39, 22 December 2014

2014-12-22T22:39:00Z

←Older revision		Revision as of 22:39, 22 December 2014
Line 31:		Line 31:
	[[Category: Methylmalonyl-CoA carboxytransferase]]		[[Category: Methylmalonyl-CoA carboxytransferase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
-	[[Category: Carey, P R.]]	+	[[Category: Carey, P R]]
-	[[Category: Reddy, D V.]]	+	[[Category: Reddy, D V]]
-	[[Category: Shenoy, B C.]]	+	[[Category: Shenoy, B C]]
-	[[Category: Sonnichsen, F D.]]	+	[[Category: Sonnichsen, F D]]
	[[Category: Antiparallel beta sheet]]		[[Category: Antiparallel beta sheet]]
	[[Category: Biocytin]]		[[Category: Biocytin]]
	[[Category: Hammerhead]]		[[Category: Hammerhead]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:25, 10 October 2014

2014-10-10T06:25:32Z

←Older revision		Revision as of 06:25, 10 October 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dcz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCZ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dd2\|1dd2]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz 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=1dcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcz RCSB], [http://www.ebi.ac.uk/pdbsum/1dcz PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]