4egh - Revision history

OCA at 11:03, 1 March 2024

2024-03-01T11:03:43Z

← Older revision		Revision as of 11:03, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4egh]] 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=4EGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EGH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4egh]] 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=4EGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EGH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.6Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [https://pdbe.org/4egh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [https://www.ebi.ac.uk/pdbsum/4egh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4egh 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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [https://pdbe.org/4egh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [https://www.ebi.ac.uk/pdbsum/4egh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4egh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>		[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	CEfrag is a new fragment screening technology based on affinity capillary electrophoresis (ACE). Here we report on the development of a mobility shift competition assay using full-length human heat shock protein 90alpha (Hsp90alpha), radicicol as the competitor probe ligand, and successful screening of the Selcia fragment library. The CEfrag assay was able to detect weaker affinity (IC(50) >500 microM) fragments than were detected by a fluorescence polarization competition assay using FITC-labeled geldanamycin. The binding site of selected fragments was determined by co-crystallization with recombinant Hsp90alpha N-terminal domain and X-ray analysis. The results of this study confirm that CEfrag is a sensitive microscale technique enabling detection of fragments binding to the biological target in near-physiological solution.

	Fragment Screening Using Capillary Electrophoresis (CEfrag) for Hit Identification of Heat Shock Protein 90 ATPase Inhibitors.,Austin C, Pettit SN, Magnolo SK, Sanvoisin J, Chen W, Wood SP, Freeman LD, Pengelly RJ, Hughes DE J Biomol Screen. 2012 May 9. PMID:22573733<ref>PMID:22573733</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4egh" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==

OCA at 07:10, 28 September 2022

2022-09-28T07:10:24Z

← Older revision		Revision as of 07:10, 28 September 2022
Line 1:		Line 1:

	==Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone==		==Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone==
	<StructureSection load='4egh' size='340' side='right' caption='[[4egh]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4egh' size='340' side='right'caption='[[4egh]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4egh]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EGH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4egh]] 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=4EGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EGH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4egi\|4egi]], [[4egk\|4egk]]</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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [https://pdbe.org/4egh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [https://www.ebi.ac.uk/pdbsum/4egh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4egh ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [~~http~~://pdbe.org/4egh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4egh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4egh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>		[[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
	*[[Heat Shock ~~Proteins~~\|Heat Shock ~~Proteins~~]]		*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Chen, W J~~]]		[[Category: Large Structures]]
	[[Category: ~~Wood, S P~~]]		[[Category: Chen WJ]]
	[[Category: ~~Atp binding]]~~		[[Category: Wood SP]]
	~~[[Category: Bergerat fold]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]

OCA at 16:13, 5 August 2016

2016-08-05T16:13:42Z

← Older revision		Revision as of 16:13, 5 August 2016
Line 1:		Line 1:

	==Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone==		==Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone==
	<StructureSection load='4egh' size='340' side='right' caption='[[4egh]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4egh' size='340' side='right' caption='[[4egh]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4egh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EGH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4egh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EGH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4egi\|4egi]], [[4egk\|4egk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4egi\|4egi]], [[4egk\|4egk]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [http://www.ebi.ac.uk/pdbsum/4egh PDBsum]</span></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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [http://pdbe.org/4egh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [http://www.ebi.ac.uk/pdbsum/4egh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4egh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4egh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Chen, W J]]		[[Category: Chen, W J]]
	[[Category: Wood, S P]]		[[Category: Wood, S P]]

OCA at 20:10, 25 December 2014

2014-12-25T20:10:03Z

← Older revision		Revision as of 20:10, 25 December 2014
Line 8:		Line 8:
	<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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [http://www.ebi.ac.uk/pdbsum/4egh PDBsum]</span></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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [http://www.ebi.ac.uk/pdbsum/4egh PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:20, 9 December 2014

2014-12-09T15:20:39Z

← Older revision		Revision as of 15:20, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4egh~~.~~png~~\|~~left~~\|~~200px~~]]		==Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone==
			<StructureSection load='4egh' size='340' side='right' caption='[[4egh]], [[Resolution\|resolution]] 1.60Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4egh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EGH FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0OY:(4-HYDROXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>0OY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4egi\|4egi]], [[4egk\|4egk]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4egh RCSB], [http://www.ebi.ac.uk/pdbsum/4egh PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			CEfrag is a new fragment screening technology based on affinity capillary electrophoresis (ACE). Here we report on the development of a mobility shift competition assay using full-length human heat shock protein 90alpha (Hsp90alpha), radicicol as the competitor probe ligand, and successful screening of the Selcia fragment library. The CEfrag assay was able to detect weaker affinity (IC(50) >500 microM) fragments than were detected by a fluorescence polarization competition assay using FITC-labeled geldanamycin. The binding site of selected fragments was determined by co-crystallization with recombinant Hsp90alpha N-terminal domain and X-ray analysis. The results of this study confirm that CEfrag is a sensitive microscale technique enabling detection of fragments binding to the biological target in near-physiological solution.

	~~{{STRUCTURE_4egh\| PDB=4egh \| SCENE= }}~~		Fragment Screening Using Capillary Electrophoresis (CEfrag) for Hit Identification of Heat Shock Protein 90 ATPase Inhibitors.,Austin C, Pettit SN, Magnolo SK, Sanvoisin J, Chen W, Wood SP, Freeman LD, Pengelly RJ, Hughes DE J Biomol Screen. 2012 May 9. PMID:22573733<ref>PMID:22573733</ref>

	~~===Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22573733}}~~		==See Also==
			*[[Heat Shock Proteins\|Heat Shock Proteins]]
	==~~About this Structure~~==		== References ==
	[[~~4egh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens~~]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGH OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:022573733<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chen, W J.]]		[[Category: Chen, W J]]
	[[Category: Wood, S P.]]		[[Category: Wood, S P]]
	[[Category: Atp binding]]		[[Category: Atp binding]]
	[[Category: Bergerat fold]]		[[Category: Bergerat fold]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 06:08, 17 October 2012

2012-10-17T06:08:34Z

← Older revision		Revision as of 06:08, 17 October 2012
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	[[Image:4egh.~~jpg~~\|left\|200px]]		[[Image:4egh.png\|left\|200px]]

	~~<!--~~
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	{{STRUCTURE_4egh\| PDB=4egh \| SCENE= }}		{{STRUCTURE_4egh\| PDB=4egh \| SCENE= }}

	===Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone===		===Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_22573733}}, adds the Publication Abstract to the page~~
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	{{ABSTRACT_PUBMED_22573733}}		{{ABSTRACT_PUBMED_22573733}}

OCA at 06:05, 23 May 2012

2012-05-23T06:05:32Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4egh.jpg|left|200px]]
-The entry 4egh is ON HOLD
+<!--
-Authors: Chen, W.J., Wood, S.P.
+===Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone===
-Description: Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone

OCA: Protected "4egh" [edit=sysop:move=sysop]

2012-04-11T06:42:23Z

Protected "4egh" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:42, 11 April 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4egh is ON HOLD Authors: Chen, W.J., Wood, S.P. Description: Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone

2012-04-11T06:42:22Z

New page: '''Unreleased structure''' The entry 4egh is ON HOLD Authors: Chen, W.J., Wood, S.P. Description: Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone

New page

'''Unreleased structure'''

The entry 4egh is ON HOLD

Authors: Chen, W.J., Wood, S.P.

Description: Hsp90-alpha ATPase domain in complex with (4-Hydroxyphenyl)morpholin-4-yl methanone