3max - Revision history

OCA at 10:24, 21 February 2024

2024-02-21T10:24:42Z

← Older revision		Revision as of 10:24, 21 February 2024
Line 1:		Line 1:

	==Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide==		==Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide==
	<StructureSection load='3max' size='340' side='right' caption='[[3max]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='3max' size='340' side='right'caption='[[3max]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3max]] 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=3MAX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MAX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3max]] 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=3MAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LLX:N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE'>LLX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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]] 2.05Å</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='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=LLX:N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE'>LLX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [https://pdbe.org/3max PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [https://www.ebi.ac.uk/pdbsum/3max PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3max ProSAT]</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=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [~~http~~://pdbe.org/3max PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3max PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3max 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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3max ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3max ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	A series of N-(2-amino-5-substituted phenyl)benzamides (3-21) were designed, synthesized and evaluated for their inhibition of HDAC2 and their cytotoxicity in HCT116 cancer cells. Multiple compounds from this series demonstrated time-dependent binding kinetics that is rationalized using a co-complex crystal structure of HDAC2 and N-(4-aminobiphenyl-3-yl)benzamide (6).

	Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides.,Bressi JC, Jennings AJ, Skene R, Wu Y, Melkus R, De Jong R, O'Connell S, Grimshaw CE, Navre M, Gangloff AR Bioorg Med Chem Lett. 2010 May 15;20(10):3142-5. Epub 2010 Mar 30. PMID:20392638<ref>PMID:20392638</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3max" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Histone deacetylase\|Histone deacetylase]]		*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Histone deacetylase~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Human~~]]		[[Category: Large Structures]]
	[[Category: Jennings~~, A J~~]]		[[Category: Jennings AJ]]
	[[Category: Skene~~, R J]]~~		[[Category: Skene RJ]]
	~~[[Category: Class 2]]~~
	~~[[Category: Foot pocket]]~~
	~~[[Category: Hdac]]~~
	~~[[Category: Hydrolase~~]]

OCA at 07:28, 9 January 2019

2019-01-09T07:28:06Z

← Older revision		Revision as of 07:28, 9 January 2019
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/3max_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/3max_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 19:01, 5 August 2016

2016-08-05T19:01:21Z

← Older revision		Revision as of 19:01, 5 August 2016
Line 1:		Line 1:

	==Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide==		==Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide==
	<StructureSection load='3max' size='340' side='right' caption='[[3max]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='3max' size='340' side='right' caption='[[3max]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3max]] is a 3 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=3MAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MAX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3max]] 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=3MAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MAX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LLX:N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE'>LLX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LLX:N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE'>LLX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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 ~~Homo sapiens~~])</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='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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [http://www.ebi.ac.uk/pdbsum/3max 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=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [http://pdbe.org/3max PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [http://www.ebi.ac.uk/pdbsum/3max PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3max ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3max ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 3max" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Jennings, A J]]		[[Category: Jennings, A J]]
	[[Category: Skene, R J]]		[[Category: Skene, R J]]

OCA at 21:10, 25 December 2014

2014-12-25T21:10:06Z

← Older revision		Revision as of 21:10, 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=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [http://www.ebi.ac.uk/pdbsum/3max 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=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [http://www.ebi.ac.uk/pdbsum/3max PDBsum]</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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:34, 9 December 2014

2014-12-09T09:34:23Z

← Older revision		Revision as of 09:34, 9 December 2014
Line 1:		Line 1:
	[[Image:~~3max~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide==
			<StructureSection load='3max' size='340' side='right' caption='[[3max]], [[Resolution\|resolution]] 2.05Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3max]] is a 3 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=3MAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MAX FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LLX:N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE'>LLX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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 Homo sapiens])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3max OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3max RCSB], [http://www.ebi.ac.uk/pdbsum/3max PDBsum]</span></td></tr>
			</table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/3max_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			A series of N-(2-amino-5-substituted phenyl)benzamides (3-21) were designed, synthesized and evaluated for their inhibition of HDAC2 and their cytotoxicity in HCT116 cancer cells. Multiple compounds from this series demonstrated time-dependent binding kinetics that is rationalized using a co-complex crystal structure of HDAC2 and N-(4-aminobiphenyl-3-yl)benzamide (6).

	~~{{STRUCTURE_3max\| PDB=3max \| SCENE= }}~~		Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides.,Bressi JC, Jennings AJ, Skene R, Wu Y, Melkus R, De Jong R, O'Connell S, Grimshaw CE, Navre M, Gangloff AR Bioorg Med Chem Lett. 2010 May 15;20(10):3142-5. Epub 2010 Mar 30. PMID:20392638<ref>PMID:20392638</ref>

	~~===Crystal Structure~~ of ~~Human HDAC2 complexed with an N-(2-aminophenyl)benzamide===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_20392638}}~~

	~~==About this Structure==~~
	~~[[3max]] is a 3 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=3MAX OCA].~~

	==See Also==		==See Also==
	*[[Histone deacetylase\|Histone deacetylase]]		*[[Histone deacetylase\|Histone deacetylase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:020392638<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Jennings, A J.]]		[[Category: Jennings, A J]]
	[[Category: Skene, R J.]]		[[Category: Skene, R J]]
	[[Category: Class 2]]		[[Category: Class 2]]
	[[Category: Foot pocket]]		[[Category: Foot pocket]]
	[[Category: Hdac]]		[[Category: Hdac]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 21:41, 20 October 2012

2012-10-20T21:41:13Z

← Older revision		Revision as of 21:41, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3max]] is a 3 chain structure ~~of [[Histone deacetylase]]~~ 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=3MAX OCA].		[[3max]] is a 3 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=3MAX OCA].

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

OCA: Protected "3max" [edit=sysop:move=sysop]

2012-07-27T13:58:56Z

Protected "3max" [edit=sysop:move=sysop]

← Older revision	Revision as of 13:58, 27 July 2012
(No difference)

OCA at 13:58, 27 July 2012

2012-07-27T13:58:55Z

← Older revision		Revision as of 13:58, 27 July 2012
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	{{STRUCTURE_3max\| PDB=3max \| SCENE= }}		{{STRUCTURE_3max\| PDB=3max \| SCENE= }}

	===Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide===		===Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide===


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	==About this Structure==		==About this Structure==
	~~3MAX~~ is a 3 ~~chains~~ structure with ~~sequences~~ 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=3MAX OCA].		[[3max]] is a 3 chain structure of [[Histone deacetylase]] 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=3MAX OCA].

			==See Also==
			*[[Histone deacetylase\|Histone deacetylase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20392638~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020392638</ref><references group="xtra"/>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
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	[[Category: Hdac]]		[[Category: Hdac]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:04:37 2010''~~

OCA at 06:04, 20 May 2010

2010-05-20T06:04:38Z

← Older revision		Revision as of 06:04, 20 May 2010
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OCA at 07:51, 28 April 2010

2010-04-28T07:51:14Z

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-'''Unreleased structure'''
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-The entry 3max is ON HOLD  until Paper Publication
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-Authors: Skene, R.J., Jennings, A.J.
+===Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide===
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