6wbw - Revision history

OCA at 14:42, 6 March 2024

OCA — Wed, 06 Mar 2024 14:42:36 GMT

←Older revision		Revision as of 14:42, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]], [[Resolution\|resolution]] 1.46Å' scene=''>		<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]], [[Resolution\|resolution]] 1.46Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6wbw]] is a 3 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=6WBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6wbw]] is a 3 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=6WBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TV1:N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide'>TV1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.46Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TV1:N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide'>TV1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </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=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [https://pdbe.org/6wbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [https://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw 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=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [https://pdbe.org/6wbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [https://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>	+	[https://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	A novel series of ethyl ketone based HDACs 1, 2, and 3 selective inhibitors have been identified with good enzymatic and cellular activity and high selectivity over HDACs 6 and 8. These inhibitors contain a spirobicyclic group in the amide region. Compound 13 stands out as a lead due to its good potency, high selectivity, and reasonable rat and dog PK. Compounds 33 and 34 show good potency and rat PK profiles as well.	+
-		+
-	Discovery of ethyl ketone-based HDACs 1, 2, and 3 selective inhibitors for HIV latency reactivation.,Yu W, Liu J, Yu Y, Zhang V, Clausen D, Kelly J, Wolkenberg S, Beshore D, Duffy JL, Chung CC, Myers RW, Klein DJ, Fells J, Holloway K, Wu J, Wu G, Howell BJ, Barnard RJO, Kozlowski J Bioorg Med Chem Lett. 2020 Apr 15:127197. doi: 10.1016/j.bmcl.2020.127197. PMID:32331932<ref>PMID:32331932</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6wbw" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 27:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone deacetylase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Klein~~, D J~~]]	+	[[Category: Klein DJ]]
-	[[Category: Yu, W]]	+	[[Category: Yu W]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]	+

OCA at 15:27, 8 June 2021

OCA — Tue, 08 Jun 2021 15:27:32 GMT

←Older revision		Revision as of 15:27, 8 June 2021
Line 3:		Line 3:
	<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]], [[Resolution\|resolution]] 1.46Å' scene=''>		<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]], [[Resolution\|resolution]] 1.46Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6wbw]] is a 3 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=6WBW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6wbw]] is a 3 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=6WBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TV1:N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide'>TV1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TV1:N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide'>TV1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [~~http~~://pdbe.org/6wbw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw 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=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [https://pdbe.org/6wbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [https://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>	+	[[https://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 6wbw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6wbw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:42, 3 June 2020

OCA — Wed, 03 Jun 2020 06:42:02 GMT

←Older revision		Revision as of 06:42, 3 June 2020
Line 1:		Line 1:

	==Structure of Human HDAC2 in complex with an ethyl ketone inhibitor==		==Structure of Human HDAC2 in complex with an ethyl ketone inhibitor==
-	<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]]' scene=''>	+	<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]], [[Resolution\|resolution]] 1.46Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WBW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6wbw]] is a 3 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=6WBW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [http://pdbe.org/6wbw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [http://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TV1:N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide'>TV1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [http://pdbe.org/6wbw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [http://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A novel series of ethyl ketone based HDACs 1, 2, and 3 selective inhibitors have been identified with good enzymatic and cellular activity and high selectivity over HDACs 6 and 8. These inhibitors contain a spirobicyclic group in the amide region. Compound 13 stands out as a lead due to its good potency, high selectivity, and reasonable rat and dog PK. Compounds 33 and 34 show good potency and rat PK profiles as well.
		+
		+	Discovery of ethyl ketone-based HDACs 1, 2, and 3 selective inhibitors for HIV latency reactivation.,Yu W, Liu J, Yu Y, Zhang V, Clausen D, Kelly J, Wolkenberg S, Beshore D, Duffy JL, Chung CC, Myers RW, Klein DJ, Fells J, Holloway K, Wu J, Wu G, Howell BJ, Barnard RJO, Kozlowski J Bioorg Med Chem Lett. 2020 Apr 15:127197. doi: 10.1016/j.bmcl.2020.127197. PMID:32331932<ref>PMID:32331932</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6wbw" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Histone deacetylase]]
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Klein DJ]]	+	[[Category: Klein, D J]]
-	[[Category: Yu W]]	+	[[Category: Yu, W]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 06:07, 6 May 2020

OCA — Wed, 06 May 2020 06:07:45 GMT

←Older revision		Revision as of 06:07, 6 May 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6wbw ~~is ON HOLD~~	+	==Structure of Human HDAC2 in complex with an ethyl ketone inhibitor==
-		+	<StructureSection load='6wbw' size='340' side='right'caption='[[6wbw]]' scene=''>
-	~~Authors~~: ~~Klein~~, D.J., Yu, W.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WBW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WBW FirstGlance]. <br>
-	~~Description: Structure of Human HDAC2 in complex with an ethyl ketone inhibitor~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wbw OCA], [http://pdbe.org/6wbw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wbw RCSB], [http://www.ebi.ac.uk/pdbsum/6wbw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wbw ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Klein~~, D.J~~]]	+	__TOC__
-	[[Category: Yu, W]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Klein DJ]]
		+	[[Category: Yu W]]

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

OCA — Wed, 08 Apr 2020 05:35:27 GMT

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

←Older revision

Revision as of 05:35, 8 April 2020

OCA: New page: '''Unreleased structure''' The entry 6wbw is ON HOLD Authors: Klein, D.J., Yu, W. Description: Structure of Human HDAC2 in complex with an ethyl ketone inhibitor [[Category: Unreleased...

OCA — Wed, 08 Apr 2020 05:35:25 GMT

New page: '''Unreleased structure''' The entry 6wbw is ON HOLD Authors: Klein, D.J., Yu, W. Description: Structure of Human HDAC2 in complex with an ethyl ketone inhibitor [[Category: Unreleased...

New page

'''Unreleased structure'''

The entry 6wbw is ON HOLD

Authors: Klein, D.J., Yu, W.

Description: Structure of Human HDAC2 in complex with an ethyl ketone inhibitor
[[Category: Unreleased Structures]]
[[Category: Klein, D.J]]
[[Category: Yu, W]]