1ub7

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<StructureSection load='1ub7' size='340' side='right'caption='[[1ub7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1ub7' size='340' side='right'caption='[[1ub7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ub7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UB7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ub7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UB7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ub7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ub7 OCA], [https://pdbe.org/1ub7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ub7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ub7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ub7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ub7 TOPSAN]</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=1ub7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ub7 OCA], [https://pdbe.org/1ub7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ub7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ub7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ub7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ub7 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q7SI99_THETH Q7SI99_THETH]] 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).[HAMAP-Rule:MF_01815]
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[https://www.uniprot.org/uniprot/Q7SI99_THETH Q7SI99_THETH] 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).[HAMAP-Rule:MF_01815]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thet8]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Inagaki, E]]
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[[Category: Inagaki E]]
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[[Category: Miyano, M]]
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[[Category: Miyano M]]
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[[Category: Structural genomic]]
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[[Category: Tahirov TH]]
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[[Category: Tahirov, T H]]
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[[Category: Beta-ketoacyl-acp synthase iii]]
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[[Category: Fabh]]
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[[Category: Fatty acid synthesis]]
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[[Category: Rsgi]]
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[[Category: Transferase]]
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Revision as of 07:31, 25 October 2023

The Crystal Analysis of Beta-Keroacyl-[Acyl Carrier Protein] Synthase III (FABH)From Thermus Thermophilus.

PDB ID 1ub7

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