4nhd - Revision history

OCA at 16:57, 20 September 2023

2023-09-20T16:57:07Z

←Older revision		Revision as of 16:57, 20 September 2023
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	<StructureSection load='4nhd' size='340' side='right'caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='4nhd' size='340' side='right'caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Vibch Vibch~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHD FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.78Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~SCY~~:~~S-ACETYL-CYSTEINE~~'>~~SCY~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">fabH1~~, ~~VC2023, VC_2023 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Beta~~-~~ketoacyl~~-~~[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180]~~ </~~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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [https://pdbe.org/4nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [https://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd 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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [https://pdbe.org/4nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [https://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).	+	[https://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).

	==See Also==		==See Also==
Line 18:		Line 16:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Vibch~~]]	+	[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
-	[[Category: Anderson~~, W F]]~~	+	[[Category: Anderson WF]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Hou J]]
-	[[Category: Hou, J]]	+	[[Category: Langner K]]
-	[[Category: Langner, K]]	+	[[Category: Minor W]]
-	[[Category: Minor, W]]	+	[[Category: Zheng H]]
-	[[Category: Zheng, H]]	+
-	~~[[Category: Csgid]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Vibrio cholerae~~]]	+

OCA at 10:04, 13 April 2022

2022-04-13T10:04:57Z

←Older revision		Revision as of 10:04, 13 April 2022
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	==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==		==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==
-	<StructureSection load='4nhd' size='340' side='right' caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>	+	<StructureSection load='4nhd' size='340' side='right'caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabH1, VC2023, VC_2023 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabH1, VC2023, VC_2023 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [~~http~~://pdbe.org/4nhd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd 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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [https://pdbe.org/4nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [https://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).	+	[[https://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).
		+
		+	==See Also==
		+	*[[Acyl carrier protein synthase 3D structures\|Acyl carrier protein synthase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Vibch]]		[[Category: Vibch]]
	[[Category: Anderson, W F]]		[[Category: Anderson, W F]]

OCA at 10:06, 15 November 2017

2017-11-15T10:06:32Z

←Older revision		Revision as of 10:06, 15 November 2017
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).		[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).
-
-	==See Also==
-	*[[Acyl carrier protein synthase\|Acyl carrier protein synthase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:14, 5 August 2016

2016-08-05T18:14:44Z

←Older revision		Revision as of 18:14, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==		==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==
	<StructureSection load='4nhd' size='340' side='right' caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='4nhd' size='340' side='right' caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabH1, VC2023, VC_2023 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabH1, VC2023, VC_2023 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd 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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://pdbe.org/4nhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).		[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).
		+
		+	==See Also==
		+	*[[Acyl carrier protein synthase\|Acyl carrier protein synthase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 04:44, 25 December 2014

2014-12-25T04:44:59Z

←Older revision		Revision as of 04:44, 25 December 2014
Line 9:		Line 9:
	<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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd 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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 16:12, 21 December 2014

2014-12-21T16:12:13Z

←Older revision		Revision as of 16:12, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4nhd\| PDB=4nhd \| SCENE= }}~~	+	==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A==
-	===Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A===	+	<StructureSection load='4nhd' size='340' side='right' caption='[[4nhd]], [[Resolution\|resolution]] 1.78Å' scene=''>
-		+	== Structural highlights ==
-	==~~Function~~==	+	<table><tr><td colspan='2'>[[4nhd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NHD FirstGlance]. <br>
-	[[~~http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH~~]] ~~Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP~~. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
-	==~~About this Structure~~==	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabH1, VC2023, VC_2023 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
-	[[4nhd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA].	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>
-	[[~~Category~~: ~~Anderson, W F~~.]]	+	<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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd PDBsum]</span></td></tr>
-	[[~~Category~~: ~~CSGID, Center for Structural Genomics of Infectious Diseases.~~]]	+	</table>
-	[[~~Category~~: ~~Hou, J.~~]]	+	__TOC__
-	[[~~Category~~: ~~Langner~~, K.]]	+	</StructureSection>
-	[~~[Category~~: ~~Minor, W~~.]]	+	[[Category: Vibch]]
-	[[~~Category~~: ~~Zheng~~, H.]]	+	[[Category: Anderson, W F]]
-	[[Category: ~~Center for structural genomics of infectious disease~~]]	+
-	[[Category: ~~Csgid~~]]	+
	[[Category: Structural genomic]]		[[Category: Structural genomic]]
		+	[[Category: Hou, J]]
		+	[[Category: Langner, K]]
		+	[[Category: Minor, W]]
		+	[[Category: Zheng, H]]
		+	[[Category: Csgid]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Vibrio cholerae]]		[[Category: Vibrio cholerae]]

OCA at 10:29, 25 December 2013

2013-12-25T10:29:22Z

←Older revision		Revision as of 10:29, 25 December 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4nhd\| PDB=4nhd \| SCENE= }}
		+	===Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A===

-	~~The entry 4nhd is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).

-	~~Authors~~: ~~Hou, J~~.~~, Zheng, H~~.~~, Langner, K~~., Anderson, W.F.~~, Minor, W.~~, Center for Structural Genomics of Infectious Diseases ~~(CSGID)~~	+	==About this Structure==
-		+	[[4nhd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHD OCA].
-	~~Description~~: ~~Crystal structure~~ of ~~beta-ketoacyl-ACP synthase III (FabH) from~~ Vibrio ~~Cholerae in complex with Coenzyme A~~	+	[[Category: Anderson, W F.]]
		+	[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
		+	[[Category: Hou, J.]]
		+	[[Category: Langner, K.]]
		+	[[Category: Minor, W.]]
		+	[[Category: Zheng, H.]]
		+	[[Category: Center for structural genomics of infectious disease]]
		+	[[Category: Csgid]]
		+	[[Category: Structural genomic]]
		+	[[Category: Transferase]]
		+	[[Category: Vibrio cholerae]]

OCA: Protected "4nhd" [edit=sysop:move=sysop]

2013-11-13T07:49:07Z

Protected "4nhd" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:49, 13 November 2013

OCA: New page: '''Unreleased structure''' The entry 4nhd is ON HOLD Authors: Hou, J., Zheng, H., Langner, K., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID) ...

2013-11-13T07:49:06Z

New page: '''Unreleased structure''' The entry 4nhd is ON HOLD Authors: Hou, J., Zheng, H., Langner, K., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID) ...

New page

'''Unreleased structure'''

The entry 4nhd is ON HOLD

Authors: Hou, J., Zheng, H., Langner, K., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)

Description: Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A