4ryb: Difference between revisions
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''' | ==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Neisseria meningitidis== | ||
<StructureSection load='4ryb' size='340' side='right' caption='[[4ryb]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ryb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qav|4qav]]</td></tr> | |||
[[Category: | <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: | <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=4ryb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ryb RCSB], [http://www.ebi.ac.uk/pdbsum/4ryb PDBsum]</span></td></tr> | ||
[[Category: | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FABH_NEIMF FABH_NEIMF]] 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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Forwood, J K]] | |||
[[Category: Nanson, J D]] | |||
[[Category: Condensing enzyme]] | |||
[[Category: Fabh]] | |||
[[Category: Kasiii]] | |||
[[Category: Thiolase fold]] | |||
[[Category: Transferase]] | |||
Revision as of 14:54, 31 December 2014
Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Neisseria meningitidis
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