2pd6: Difference between revisions

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<StructureSection load='2pd6' size='340' side='right'caption='[[2pd6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2pd6' size='340' side='right'caption='[[2pd6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pd6]] is a 4 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=2PD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PD6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pd6]] is a 4 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=2PD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PD6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSD17B8, FABGL, HKE6, RING2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pd6 OCA], [https://pdbe.org/2pd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pd6 RCSB], [https://www.ebi.ac.uk/pdbsum/2pd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pd6 ProSAT]</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=2pd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pd6 OCA], [https://pdbe.org/2pd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pd6 RCSB], [https://www.ebi.ac.uk/pdbsum/2pd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pd6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DHB8_HUMAN DHB8_HUMAN]] NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone. The heteroteramer with CBR4 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria.<ref>PMID:17978863</ref> <ref>PMID:19571038</ref>
[https://www.uniprot.org/uniprot/DHB8_HUMAN DHB8_HUMAN] NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone. The heteroteramer with CBR4 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria.<ref>PMID:17978863</ref> <ref>PMID:19571038</ref>  
== 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: 17-beta-estradiol 17-dehydrogenase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bunkoczi, G]]
[[Category: Bunkoczi G]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Gileadi O]]
[[Category: Gileadi, O]]
[[Category: Guo K]]
[[Category: Guo, K]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Pike ACW]]
[[Category: Pike, A C.W]]
[[Category: Salah E]]
[[Category: Structural genomic]]
[[Category: Savitsky P]]
[[Category: Salah, E]]
[[Category: Sundstrom M]]
[[Category: Savitsky, P]]
[[Category: Turnbull AP]]
[[Category: Sundstrom, M]]
[[Category: Ugochukwu E]]
[[Category: Turnbull, A P]]
[[Category: Umeano C]]
[[Category: Ugochukwu, E]]
[[Category: Weigelt J]]
[[Category: Umeano, C]]
[[Category: Von Delft F]]
[[Category: Weigelt, J]]
[[Category: Lipid metabolism]]
[[Category: Oxidoreductase]]
[[Category: Sgc]]
[[Category: Short-chain dehydrogenase/reductase]]
[[Category: Steroid metabolism]]

Latest revision as of 10:59, 30 August 2023

Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8

2pd6, resolution 2.00Å

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