1xkt: Difference between revisions

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 <StructureSection load='1xkt' size='340' side='right'caption='[[1xkt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xkt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xkt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKT FirstGlance]. <br>
-</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=1xkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkt OCA], [https://pdbe.org/1xkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xkt RCSB], [https://www.ebi.ac.uk/pdbsum/1xkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkt ProSAT]</span></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]] 2.6&#8491;</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=1xkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkt OCA], [https://pdbe.org/1xkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xkt RCSB], [https://www.ebi.ac.uk/pdbsum/1xkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
+[https://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xkt ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Human fatty acid synthase is a large homodimeric multifunctional enzyme that synthesizes palmitic acid. The unique carboxyl terminal thioesterase domain of fatty acid synthase hydrolyzes the growing fatty acid chain and plays a critical role in regulating the chain length of fatty acid released. Also, the up-regulation of human fatty acid synthase in a variety of cancer makes the thioesterase a candidate target for therapeutic treatment. The 2.6-A resolution structure of human fatty acid synthase thioesterase domain reported here is comprised of two dissimilar subdomains, A and B. The smaller subdomain B is composed entirely of alpha-helices arranged in an atypical fold, whereas the A subdomain is a variation of the alpha/beta hydrolase fold. The structure revealed the presence of a hydrophobic groove with a distal pocket at the interface of the two subdomains, which constitutes the candidate substrate binding site. The length and largely hydrophobic nature of the groove and pocket are consistent with the high selectivity of the thioesterase for palmitoyl acyl substrate. The structure also set the identity of the Asp residue of the catalytic triad of Ser, His, and Asp located in subdomain A at the proximal end of the groove.
-Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain.,Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15567-72. Epub 2004 Oct 26. PMID:15507492<ref>PMID:15507492</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1xkt" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Chakravarty, B]]
+[[Category: Chakravarty B]]
-[[Category: Chirala, S S]]
+[[Category: Chirala SS]]
-[[Category: Gu, Z]]
+[[Category: Gu Z]]
-[[Category: Quiocho, F A]]
+[[Category: Quiocho FA]]
-[[Category: Wakil, S J]]
+[[Category: Wakil SJ]]
-[[Category: Drug target]]
-[[Category: Human fatty acid synthase]]
-[[Category: Hydroxylase]]
-[[Category: Specificity]]
-[[Category: Thioesterase]]