5kco - Revision history

OCA at 09:58, 27 September 2023

OCA — Wed, 27 Sep 2023 09:58:14 GMT

←Older revision		Revision as of 09:58, 27 September 2023
Line 3:		Line 3:
	<StructureSection load='5kco' size='340' side='right'caption='[[5kco]], [[Resolution\|resolution]] 1.47Å' scene=''>		<StructureSection load='5kco' size='340' side='right'caption='[[5kco]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kco]] 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=5KCO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5KCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kco]] 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=5KCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KCO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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]] 1.47Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kch\|5kch]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETDB1, KIAA0067, KMT1E ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [https://pdbe.org/5kco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [https://www.ebi.ac.uk/pdbsum/5kco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [~~http~~://pdbe.org/5kco PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5kco PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>	+	[https://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>

	==See Also==		==See Also==
Line 19:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone-lysine N-methyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Brandao-Neto, J]]	+	[[Category: Brandao-Neto J]]
-	[[Category: Brown~~, P J~~]]	+	[[Category: Brown PJ]]
-	[[Category: Collins, P]]	+	[[Category: Collins P]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Dobrovetsky E]]
-	[[Category: Dobrovetsky, E]]	+	[[Category: Douangamath A]]
-	[[Category: Douangamath, A]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Harding RJ]]
-	[[Category: Harding~~, R J~~]]	+	[[Category: Mader P]]
-	[[Category: Mader, P]]	+	[[Category: Pearce N]]
-	[[Category: Pearce, N]]	+	[[Category: Santhakumar V]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Schapira M]]
-	[[Category: Santhakumar, V]]	+	[[Category: Tempel W]]
-	[[Category: Schapira, M]]	+	[[Category: Walker JR]]
-	[[Category: Tempel, W]]	+	[[Category: Von Delft F]]
-	[[Category: Walker~~, J R~~]]	+
-	[[Category: ~~Diamond i04-1 xchem]]~~	+
-	~~[[Category: Fragment screening]]~~	+
-	~~[[Category: Pandda]]~~	+
-	~~[[Category: Sgc]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:34, 1 July 2020

OCA — Wed, 01 Jul 2020 09:34:22 GMT

←Older revision		Revision as of 09:34, 1 July 2020
Line 1:		Line 1:

	==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy==		==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy==
-	<StructureSection load='5kco' size='340' side='right' caption='[[5kco]], [[Resolution\|resolution]] 1.47Å' scene=''>	+	<StructureSection load='5kco' size='340' side='right'caption='[[5kco]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kco]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCO OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5KCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kco]] 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=5KCO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KCO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kch\|5kch]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kch\|5kch]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETDB1, KIAA0067, KMT1E ([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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [http://pdbe.org/5kco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [http://www.ebi.ac.uk/pdbsum/5kco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</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=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [http://pdbe.org/5kco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [http://www.ebi.ac.uk/pdbsum/5kco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>		[[http://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 16:		Line 20:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Bountra, C]]		[[Category: Bountra, C]]

OCA at 15:47, 27 July 2016

OCA — Wed, 27 Jul 2016 15:47:24 GMT

←Older revision		Revision as of 15:47, 27 July 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5kco ~~is ON HOLD until Sep 20 2017~~	+	==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy==
-		+	<StructureSection load='5kco' size='340' side='right' caption='[[5kco]], [[Resolution\|resolution]] 1.47Å' scene=''>
-	~~Authors~~: ~~Tempel, W~~.~~, Harding, R~~.J.~~, Mader, P~~.~~, Dobrovetsky, E~~.~~, Walker, J~~.R., ~~Brown~~, P.J., ~~Schapira, M~~., ~~Arrowsmith, C~~.H., ~~Edwards~~, A.M., ~~Santhakumar, S~~., ~~Structural Genomics Consortium (SGC)~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5kco]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KCO FirstGlance]. <br>
-	~~Description~~: ~~SETDB1~~ in complex with ~~an early stage~~, ~~low affinity fragment candidate modelled at reduced occupancy~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kch\|5kch]]</td></tr>
-	[[Category: ~~Schapira~~, M]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
-	[[Category: ~~Walker~~, J.R]]	+	<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=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [http://pdbe.org/5kco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [http://www.ebi.ac.uk/pdbsum/5kco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Arrowsmith, C H]]
		+	[[Category: Bountra, C]]
		+	[[Category: Brandao-Neto, J]]
		+	[[Category: Brown, P J]]
		+	[[Category: Collins, P]]
		+	[[Category: Delft, F von]]
	[[Category: Dobrovetsky, E]]		[[Category: Dobrovetsky, E]]
		+	[[Category: Douangamath, A]]
		+	[[Category: Edwards, A M]]
		+	[[Category: Harding, R J]]
	[[Category: Mader, P]]		[[Category: Mader, P]]
		+	[[Category: Pearce, N]]
		+	[[Category: Structural genomic]]
		+	[[Category: Santhakumar, V]]
		+	[[Category: Schapira, M]]
	[[Category: Tempel, W]]		[[Category: Tempel, W]]
-	[[Category: ~~Arrowsmith~~, ~~C.H~~]]	+	[[Category: Walker, J R]]
-	[[Category: ~~Brown, P.J~~]]	+	[[Category: Diamond i04-1 xchem]]
-	[[Category: ~~Santhakumar, S~~]]	+	[[Category: Fragment screening]]
-	[[Category: ~~Edwards, A.M~~]]	+	[[Category: Pandda]]
-	[[Category: ~~Structural Genomics Consortium (~~Sgc)]]	+	[[Category: Sgc]]
-	[[Category: ~~Harding, R.J~~]]	+	[[Category: Transferase]]

OCA at 00:14, 13 July 2016

OCA — Wed, 13 Jul 2016 00:14:51 GMT

←Older revision		Revision as of 00:14, 13 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5kco is ON HOLD	+	The entry 5kco is ON HOLD until Sep 20 2017

	Authors: Tempel, W., Harding, R.J., Mader, P., Dobrovetsky, E., Walker, J.R., Brown, P.J., Schapira, M., Arrowsmith, C.H., Edwards, A.M., Santhakumar, S., Structural Genomics Consortium (SGC)		Authors: Tempel, W., Harding, R.J., Mader, P., Dobrovetsky, E., Walker, J.R., Brown, P.J., Schapira, M., Arrowsmith, C.H., Edwards, A.M., Santhakumar, S., Structural Genomics Consortium (SGC)

OCA: Protected "5kco" [edit=sysop:move=sysop]

OCA — Mon, 20 Jun 2016 13:44:45 GMT

Protected "5kco" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:44, 20 June 2016

OCA: New page: '''Unreleased structure''' The entry 5kco is ON HOLD Authors: Tempel, W., Harding, R.J., Mader, P., Dobrovetsky, E., Walker, J.R., Brown, P.J., Schapira, M., Arrowsmith, C.H., Edwards, ...

OCA — Mon, 20 Jun 2016 13:44:43 GMT

New page: '''Unreleased structure''' The entry 5kco is ON HOLD Authors: Tempel, W., Harding, R.J., Mader, P., Dobrovetsky, E., Walker, J.R., Brown, P.J., Schapira, M., Arrowsmith, C.H., Edwards, ...

New page

'''Unreleased structure'''

The entry 5kco is ON HOLD

Authors: Tempel, W., Harding, R.J., Mader, P., Dobrovetsky, E., Walker, J.R., Brown, P.J., Schapira, M., Arrowsmith, C.H., Edwards, A.M., Santhakumar, S., Structural Genomics Consortium (SGC)

Description: SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy
[[Category: Unreleased Structures]]
[[Category: Schapira, M]]
[[Category: Walker, J.R]]
[[Category: Dobrovetsky, E]]
[[Category: Mader, P]]
[[Category: Tempel, W]]
[[Category: Arrowsmith, C.H]]
[[Category: Brown, P.J]]
[[Category: Santhakumar, S]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]
[[Category: Harding, R.J]]