4x9o
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae soaked with octanoyl-CoA: conformational changes without clearly bound substrate== |
| - | + | <StructureSection load='4x9o' size='340' side='right' caption='[[4x9o]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4x9o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X9O FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wzu|4wzu]], [[4x0o|4x0o]], [[4x9k|4x9k]]</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=4x9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x9o RCSB], [http://www.ebi.ac.uk/pdbsum/4x9o PDBsum]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_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.[HAMAP-Rule:MF_01815] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Anderson, W F]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Cooper, D R]] | ||
| + | [[Category: Grabowski, M]] | ||
| + | [[Category: Hou, J]] | ||
[[Category: Minor, W]] | [[Category: Minor, W]] | ||
| + | [[Category: Shabalin, I G]] | ||
[[Category: Shumilin, I]] | [[Category: Shumilin, I]] | ||
| - | [[Category: | + | [[Category: Beta-ketoacyl-acyl carrier protein synthase iii]] |
| - | [[Category: | + | [[Category: Csgid]] |
| - | [[Category: | + | [[Category: Fabh]] |
| - | + | [[Category: Transferase]] | |
| - | [[Category: | + | |
Revision as of 12:00, 11 March 2015
Beta-ketoacyl-ACP synthase III -2 (FabH2) (C113A) from Vibrio Cholerae soaked with octanoyl-CoA: conformational changes without clearly bound substrate
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