5hs6: Difference between revisions

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-'''Unreleased structure'''
-The entry 5hs6 is ON HOLD  until Paper Publication
+==Human 17beta-hydroxysteroid dehydrogenase type 14 in complex with Estrone==
+<StructureSection load='5hs6' size='340' side='right' caption='[[5hs6]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5hs6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HS6 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=J3Z:(9BETA,13ALPHA)-3-HYDROXYESTRA-1,3,5(10)-TRIEN-17-ONE'>J3Z</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5en4|5en4]]</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=5hs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hs6 OCA], [http://pdbe.org/5hs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hs6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hs6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hs6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DHB14_HUMAN DHB14_HUMAN]] Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro).<ref>PMID:17067289</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+beta-HSD14 is a SDR enzyme able to oxidize estradiol and 5-androstenediol using NAD+. We determined the crystal structure of this human enzyme as the holo form and as ternary complexes with estrone and with the first potent, nonsteroidal inhibitor. The structures reveal a conical, rather large and lipophilic binding site and are the starting point for structure-based inhibitor design. The two natural variants (S205 and T205) were characterized and adopt a similar structure.
-Authors: Bertoletti, N., Marchais-Oberwinkler, S., Heine, A., Klebe, G.
+New Insights into Human 17beta-Hydroxysteroid Dehydrogenase Type 14: First Crystal Structures in Complex with a Steroidal Ligand and with a Potent Nonsteroidal Inhibitor.,Bertoletti N, Braun F, Lepage M, Moller G, Adamski J, Heine A, Klebe G, Marchais-Oberwinkler S J Med Chem. 2016 Jul 12. PMID:27362750<ref>PMID:27362750</ref>
-Description: Human 17beta-hydroxysteroid dehydrogenase type 14 in complex with Estrone
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5hs6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bertoletti, N]]
+[[Category: Heine, A]]
+[[Category: Klebe, G]]
 [[Category: Marchais-Oberwinkler, S]]
-[[Category: Klebe, G]]
+[[Category: Estrone complex]]
-[[Category: Heine, A]]
+[[Category: Oxidoreductase]]
-[[Category: Bertoletti, N]]