4nhd
From Proteopedia
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| - | {{STRUCTURE_4nhd| PDB=4nhd | SCENE= }} | ||
| - | ===Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A=== | ||
| - | == | + | ==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A== |
| - | [[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH | + | <StructureSection load='4nhd' size='340' side='right'caption='[[4nhd]], [[Resolution|resolution]] 1.78Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4nhd]] is a 4 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=4NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHD 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]] 1.78Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [https://pdbe.org/4nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [https://www.ebi.ac.uk/pdbsum/4nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_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 (By similarity). | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Hou | + | [[Category: Large Structures]] |
| - | [[Category: Langner | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
| - | [[Category: Minor | + | [[Category: Anderson WF]] |
| - | [[Category: Zheng | + | [[Category: Hou J]] |
| - | + | [[Category: Langner K]] | |
| - | + | [[Category: Minor W]] | |
| - | + | [[Category: Zheng H]] | |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A
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