4z8d: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry 4z8d is ON HOLD until Paper Publication~~

==Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping==

~~Authors: Lahiri, S.D.~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4z8d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z8D OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z8D FirstGlance].

~~Description:~~ Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=4LB:TRANS-4-[({[(2-CHLOROBENZYL)OXY]CARBONYL}AMINO)METHYL]CYCLOHEXANECARBOXYLIC+ACID'>4LB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

[[~~Category~~: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: Lahiri, S.D]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z8d OCA], [http://pdbe.org/4z8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z8d RCSB], [http://www.ebi.ac.uk/pdbsum/4z8d PDBsum]</td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/FABH_ECO57 FABH_ECO57]] 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.[HAMAP-Rule:MF_01815]

__TOC__

</StructureSection>

[[Category: Lahiri, S D]]

[[Category: Carbamate]]

[[Category: Fatty acid biosynthesis]]

[[Category: Structure based drug design]]

[[Category: Transferase-transferase inhibitor complex]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4z8d is ON HOLD  until Paper Publication
+==Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping==
+<StructureSection load='4z8d' size='340' side='right' caption='[[4z8d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-Authors: Lahiri, S.D.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4z8d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z8D FirstGlance]. <br>
-Description: Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4LB:TRANS-4-[({[(2-CHLOROBENZYL)OXY]CARBONYL}AMINO)METHYL]CYCLOHEXANECARBOXYLIC+ACID'>4LB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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: Lahiri, S.D]]
+<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=4z8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z8d OCA], [http://pdbe.org/4z8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z8d RCSB], [http://www.ebi.ac.uk/pdbsum/4z8d PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FABH_ECO57 FABH_ECO57]] 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.[HAMAP-Rule:MF_01815]
+__TOC__
+</StructureSection>
+[[Category: Lahiri, S D]]
+[[Category: Carbamate]]
+[[Category: Fatty acid biosynthesis]]
+[[Category: Structure based drug design]]
+[[Category: Transferase-transferase inhibitor complex]]