2hq1: Difference between revisions

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<StructureSection load='2hq1' size='340' side='right'caption='[[2hq1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2hq1' size='340' side='right'caption='[[2hq1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQ1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2hq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQ1 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/17-beta-estradiol_17-dehydrogenase 17-beta-estradiol 17-dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62] </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]] 1.9&#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=2hq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hq1 OCA], [https://pdbe.org/2hq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2hq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hq1 ProSAT], [https://www.topsan.org/Proteins/SECSG/2hq1 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=2hq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hq1 OCA], [https://pdbe.org/2hq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2hq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hq1 ProSAT], [https://www.topsan.org/Proteins/SECSG/2hq1 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A3DDY9_ACET2 A3DDY9_ACET2] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[RuleBase:RU366074]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ruminiclostridium thermocellum yutin and galperin 2013]]
[[Category: Acetivibrio thermocellus]]
[[Category: 17-beta-estradiol 17-dehydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, L]]
[[Category: Chen L]]
[[Category: Cheng, C]]
[[Category: Cheng C]]
[[Category: Li, Y]]
[[Category: Li Y]]
[[Category: Liu, Z J]]
[[Category: Liu ZJ]]
[[Category: Rose, J P]]
[[Category: Rose JP]]
[[Category: Structural genomic]]
[[Category: Shaw N]]
[[Category: Shaw, N]]
[[Category: Wang BC]]
[[Category: Wang, B C]]
[[Category: Xu H]]
[[Category: Xu, H]]
[[Category: Cth-1438]]
[[Category: Glucose/ribitol dehydrogenase]]
[[Category: Oxidoreductase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Secsg]]
Retrieved from "https://proteopedia.org/2hq1"