5v0p
From Proteopedia
(Difference between revisions)
(2 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of Beta-ketoacyl-ACP synthase III-2 (FabH2) (C113A) from Vibrio Cholerae co-crystallized with octanoyl-CoA== | |
+ | <StructureSection load='5v0p' size='340' side='right'caption='[[5v0p]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5v0p]] is a 2 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=5V0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V0P FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO8:OCTANOYL-COENZYME+A'>CO8</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5v0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v0p OCA], [https://pdbe.org/5v0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v0p RCSB], [https://www.ebi.ac.uk/pdbsum/5v0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v0p ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://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] | ||
- | + | ==See Also== | |
- | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | |
- | + | __TOC__ | |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
- | [[Category: | + | [[Category: Anderson WF]] |
- | [[Category: Grabowski | + | [[Category: Cooper DR]] |
- | [[Category: | + | [[Category: Grabowski M]] |
- | [[Category: | + | [[Category: Hou J]] |
- | [[Category: | + | [[Category: Minor W]] |
+ | [[Category: Zheng H]] |
Current revision
Crystal Structure of Beta-ketoacyl-ACP synthase III-2 (FabH2) (C113A) from Vibrio Cholerae co-crystallized with octanoyl-CoA
|