5bns

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'''Unreleased structure'''
 
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The entry 5bns is ON HOLD until Paper Publication
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==E. coli Fabh with small molecule inhibitor 2==
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<StructureSection load='5bns' size='340' side='right' caption='[[5bns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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Authors: Kazmirski, S.L., McKinney, D.C.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bns]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BNS FirstGlance]. <br>
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Description: E. coli Fabh with small molecule inhibitor 2
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4VM:1-{5-[2-FLUORO-5-(HYDROXYMETHYL)PHENYL]PYRIDIN-2-YL}-N-(QUINOLIN-6-YLMETHYL)PIPERIDINE-4-CARBOXAMIDE'>4VM</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bnm|5bnm]], [[5bnr|5bnr]], [[5bqs|5bqs]]</td></tr>
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[[Category: Mckinney, D.C]]
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<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>
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[[Category: Kazmirski, S.L]]
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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=5bns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bns OCA], [http://pdbe.org/5bns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bns RCSB], [http://www.ebi.ac.uk/pdbsum/5bns PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI]] 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
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__TOC__
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</StructureSection>
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[[Category: Kazmirski, S L]]
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[[Category: McKinney, D C]]
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[[Category: Anti-bacterial]]
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[[Category: Fabh]]
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[[Category: Fatty acid synthesis]]
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[[Category: Transferase-transferase inhibitor complex]]

Revision as of 15:48, 1 June 2016

E. coli Fabh with small molecule inhibitor 2

5bns, resolution 2.20Å

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