5v0p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal Structure of Beta-ketoacyl-ACP synthase III-2 (FabH2) (C113A) from Vibrio Cholerae co-crystallized with octanoyl-CoA==
==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]] 2.16&Aring;' scene=''>
<StructureSection load='5v0p' size='340' side='right'caption='[[5v0p]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5v0p]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V0P FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO8:OCTANOYL-COENZYME+A'>CO8</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v0p OCA], [http://pdbe.org/5v0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v0p RCSB], [http://www.ebi.ac.uk/pdbsum/5v0p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v0p ProSAT]</span></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>
</table>
== Function ==
== 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]  
[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__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anderson, W F]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Cooper, D R]]
[[Category: Anderson WF]]
[[Category: Grabowski, M]]
[[Category: Cooper DR]]
[[Category: Hou, J]]
[[Category: Grabowski M]]
[[Category: Minor, W]]
[[Category: Hou J]]
[[Category: Zheng, H]]
[[Category: Minor W]]
[[Category: Beta-ketoacyl-acyl carrier protein synthase iii]]
[[Category: Zheng H]]
[[Category: Csgid]]
[[Category: Fabh]]
[[Category: Octanoyl-coa]]
[[Category: Transferase]]