6hno - Revision history

OCA at 11:33, 24 January 2024

OCA — Wed, 24 Jan 2024 11:33:51 GMT

←Older revision		Revision as of 11:33, 24 January 2024
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	<StructureSection load='6hno' size='340' side='right'caption='[[6hno]], [[Resolution\|resolution]] 1.68Å' scene=''>		<StructureSection load='6hno' size='340' side='right'caption='[[6hno]], [[Resolution\|resolution]] 1.68Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6hno]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HNO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6HNO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6hno]] is a 1 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=6HNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HNO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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]] 1.68Å</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=6hno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hno OCA], [~~http~~://pdbe.org/6hno PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6hno RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6hno PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6hno ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hno OCA], [https://pdbe.org/6hno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hno RCSB], [https://www.ebi.ac.uk/pdbsum/6hno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hno ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>	+	[https://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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 6hno" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6hno" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hydroxysteroid dehydrogenase 3D structures\|Hydroxysteroid dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bertoletti, N]]	+	[[Category: Bertoletti N]]
-	[[Category: Heine, A]]	+	[[Category: Heine A]]
-	[[Category: Klebe, G]]	+	[[Category: Klebe G]]
-	[[Category: Marchais-Oberwinkler, S]]	+	[[Category: Marchais-Oberwinkler S]]
-	~~[[Category: 17b-hsd14]]~~	+
-	~~[[Category: Inhibition]]~~	+
-	~~[[Category: Mutation]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 06:15, 31 July 2019

OCA — Wed, 31 Jul 2019 06:15:28 GMT

←Older revision		Revision as of 06:15, 31 July 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6hno is ~~ON HOLD~~	+	==17beta-hydroxysteroid dehydrogenase 14 variant S205 - mutant H93A==
		+	<StructureSection load='6hno' size='340' side='right'caption='[[6hno]], [[Resolution\|resolution]] 1.68Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6hno]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HNO FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=6hno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hno OCA], [http://pdbe.org/6hno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hno RCSB], [http://www.ebi.ac.uk/pdbsum/6hno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hno 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 ==
		+	17beta-Hydroxysteroid dehydrogenase type 14 (17beta-HSD14) catalyzes the conversion of highly active estrogens and androgens into their less active oxidized forms in presence of NAD(+) as cofactor. The crystal structure of 17beta-HSD14 has been determined, however, the role of individual amino acids likely involved in the enzymatic function remains poorly understood. Objective of this study was to further characterize the enzyme by site-directed mutagenesis considering five amino acids next to the catalytic center. The tools used for the characterization of the enzyme variants are X-ray crystallography and enzyme kinetics. Lys158 was confirmed to belong to the catalytic triad. Tyr253', located on the C-terminal loop of the adjacent monomer, enters into the active site of the neighboring monomer and interacts with the catalytic Tyr154. Therefore, Tyr253' helps to tie the two monomers together. Cys255, located at the interface between both monomers, can form a disulfide bridge with the Cys255' from the adjacent monomer. In contrast to the contact provided by Tyr253, the latter interaction is not crucial for dimer formation. His93 and Gln148 are located at the rim of the substrate binding pocket. His93 does not interact directly with the ligand in the active site. However, it influences the turnover of the enzyme. The Gln148 restricts in size the access tunnel of the substrate to the binding pocket.

-	~~Authors~~:	+	Mutational and structural studies uncover crucial amino acids determining activity and stability of 17beta-HSD14.,Badran MJ, Bertoletti N, Keils A, Heine A, Klebe G, Marchais-Oberwinkler S J Steroid Biochem Mol Biol. 2019 May;189:135-144. doi:, 10.1016/j.jsbmb.2019.02.009. Epub 2019 Mar 2. PMID:30836176<ref>PMID:30836176</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6hno" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bertoletti, N]]
		+	[[Category: Heine, A]]
		+	[[Category: Klebe, G]]
		+	[[Category: Marchais-Oberwinkler, S]]
		+	[[Category: 17b-hsd14]]
		+	[[Category: Inhibition]]
		+	[[Category: Mutation]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "6hno" [edit=sysop:move=sysop]

OCA — Wed, 26 Sep 2018 06:13:16 GMT

Protected "6hno" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:13, 26 September 2018

OCA: New page: '''Unreleased structure''' The entry 6hno is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 26 Sep 2018 06:13:15 GMT

New page: '''Unreleased structure''' The entry 6hno is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6hno is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]