5fyq - Revision history

OCA at 13:32, 26 July 2023

OCA — Wed, 26 Jul 2023 13:32:12 GMT

←Older revision		Revision as of 13:32, 26 July 2023
Line 3:		Line 3:
	<StructureSection load='5fyq' size='340' side='right'caption='[[5fyq]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='5fyq' size='340' side='right'caption='[[5fyq]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fyq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5FYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fyq]] is a 4 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=5FYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FYQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</scene></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [~~http~~://pdbe.org/5fyq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fyq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyq 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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [https://pdbe.org/5fyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [https://www.ebi.ac.uk/pdbsum/5fyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN]] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref> [[http://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>	+	[https://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baldus, L]]	+	[[Category: Baldus L]]
-	[[Category: Baumann, U]]	+	[[Category: Baumann U]]
-	~~[[Category: Boor, S de~~]]	+	[[Category: Extra A]]
-	[[Category: Extra, A]]	+	[[Category: Knyphausen P]]
-	[[Category: Knyphausen, P]]	+	[[Category: Lammers M]]
-	[[Category: Lammers, M]]	+	[[Category: Neundorf I]]
-	[[Category: Neundorf, I]]	+	[[Category: Schacherl M]]
-	[[Category: Schacherl, M]]	+	[[Category: Scislowski L]]
-	[[Category: Scislowski, L]]	+	[[Category: De Boor S]]
-	[[Category: ~~Genetic-code expansion]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Kdac]]~~	+
-	~~[[Category: Lysine-acetylation]]~~	+
-	~~[[Category: Lysine-deacetylase]]~~	+
-	~~[[Category: Sirtuin~~]]	+

OCA at 06:30, 13 May 2020

OCA — Wed, 13 May 2020 06:30:14 GMT

←Older revision		Revision as of 06:30, 13 May 2020
Line 1:		Line 1:

	==Sirt2 in complex with a 13-mer trifluoroacetylated Ran peptide==		==Sirt2 in complex with a 13-mer trifluoroacetylated Ran peptide==
-	<StructureSection load='5fyq' size='340' side='right' caption='[[5fyq]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='5fyq' size='340' side='right'caption='[[5fyq]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fyq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fyq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FYQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [http://pdbe.org/5fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [http://www.ebi.ac.uk/pdbsum/5fyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyq 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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [http://pdbe.org/5fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [http://www.ebi.ac.uk/pdbsum/5fyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5fyq" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fyq" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Baldus, L]]		[[Category: Baldus, L]]
	[[Category: Baumann, U]]		[[Category: Baumann, U]]

OCA at 08:06, 27 July 2016

OCA — Wed, 27 Jul 2016 08:06:41 GMT

←Older revision		Revision as of 08:06, 27 July 2016
Line 6:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [http://pdbe.org/5fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [http://www.ebi.ac.uk/pdbsum/5fyq 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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [http://pdbe.org/5fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [http://www.ebi.ac.uk/pdbsum/5fyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fyq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 08:05, 20 June 2016

OCA — Mon, 20 Jun 2016 08:05:14 GMT

←Older revision		Revision as of 08:05, 20 June 2016
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN]] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref> [[http://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>		[[http://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN]] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref> [[http://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Sirtuins are NAD+ dependent lysine-deacylases, regulating a variety of cellular processes. The nuclear Sirt1, the cytosolic Sirt2 and the mitochondrial Sirt3 are robust deacetylases, whereas the other sirtuins have preferences for longer acylchains. Most previous studies investigated sirtuin-catalysed deacylation on peptide substrates only. We used the genetic code expansion concept to produce natively folded site-specifically lysine acetylated Sirt1-3 substrate proteins, namely Ran, p53, PEPCK1, MnSOD, CypD and Hsp10, and analysed the deacetylation reaction. Some acetylated proteins such as Ran, p53 and Hsp10 were robustly deacetylated by Sirt1-3. However, other reported sirtuin substrate proteins such as CypD, MnSOD and PEPCK1, were not deacetylated. Using a structural and functional approach, we describe the ability of Sirt1-3 to deacetylate two adjacent acetylated lysine residues. The dynamics of this process has implications for the lifetime of acetyl-modifications on di-lysine-acetylation sites and thus constitutes a new mechanism for the regulation of proteins by acetylation. Our studies support that, besides the primary sequence-context, the protein structure is a major determinant of sirtuin substrate specificity.
		+
		+	Insights into lysine-deacetylation of natively folded substrate proteins by sirtuins.,Knyphausen P, de Boor S, Kuhlmann N, Scislowski L, Extra A, Baldus L, Schacherl M, Baumann U, Neundorf I, Lammers M J Biol Chem. 2016 May 18. pii: jbc.M116.726307. PMID:27226597<ref>PMID:27226597</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5fyq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:58, 1 June 2016

OCA — Wed, 01 Jun 2016 22:58:01 GMT

←Older revision		Revision as of 22:58, 1 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5fyq ~~is ON HOLD until Paper Publication~~	+	==Sirt2 in complex with a 13-mer trifluoroacetylated Ran peptide==
-		+	<StructureSection load='5fyq' size='340' side='right' caption='[[5fyq]], [[Resolution\|resolution]] 3.00Å' scene=''>
-	~~Authors~~: ~~Knyphausen, P~~.~~, de Boor, S~~.~~, Scislowski, L~~.~~, Extra, A~~., ~~Baldus,~~ L.~~, Schacherl, M~~., ~~Baumann~~, U., ~~Neundorf, I~~., ~~Lammers, M~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5fyq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FYQ FirstGlance]. <br>
-	~~Description~~: ~~Sirt2~~ in ~~complex with a 13~~-~~mer trifluoroacetylated Ran peptide~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAK:N~6~-(TRIFLUOROACETYL)-L-LYSINE'>FAK</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=5fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fyq OCA], [http://pdbe.org/5fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fyq RCSB], [http://www.ebi.ac.uk/pdbsum/5fyq PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN]] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref> [[http://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Baldus, L]]		[[Category: Baldus, L]]
		+	[[Category: Baumann, U]]
		+	[[Category: Boor, S de]]
	[[Category: Extra, A]]		[[Category: Extra, A]]
-	[[Category: Scislowski, L]]
	[[Category: Knyphausen, P]]		[[Category: Knyphausen, P]]
		+	[[Category: Lammers, M]]
	[[Category: Neundorf, I]]		[[Category: Neundorf, I]]
-	[[Category: De Boor, S]]
-	[[Category: Baumann, U]]
	[[Category: Schacherl, M]]		[[Category: Schacherl, M]]
-	[[Category: ~~Lammers~~, M]]	+	[[Category: Scislowski, L]]
		+	[[Category: Genetic-code expansion]]
		+	[[Category: Hydrolase]]
		+	[[Category: Kdac]]
		+	[[Category: Lysine-acetylation]]
		+	[[Category: Lysine-deacetylase]]
		+	[[Category: Sirtuin]]

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

OCA — Tue, 10 May 2016 23:15:09 GMT

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

←Older revision

Revision as of 23:15, 10 May 2016

OCA: New page: '''Unreleased structure''' The entry 5fyq is ON HOLD until Paper Publication Authors: Knyphausen, P., de Boor, S., Scislowski, L., Extra, A., Baldus, L., Schacherl, M., Baumann, U., Neu...

OCA — Tue, 10 May 2016 23:15:08 GMT

New page: '''Unreleased structure''' The entry 5fyq is ON HOLD until Paper Publication Authors: Knyphausen, P., de Boor, S., Scislowski, L., Extra, A., Baldus, L., Schacherl, M., Baumann, U., Neu...

New page

'''Unreleased structure'''

The entry 5fyq is ON HOLD until Paper Publication

Authors: Knyphausen, P., de Boor, S., Scislowski, L., Extra, A., Baldus, L., Schacherl, M., Baumann, U., Neundorf, I., Lammers, M.

Description: Sirt2 in complex with a 13-mer trifluoroacetylated Ran peptide
[[Category: Unreleased Structures]]
[[Category: Baldus, L]]
[[Category: Extra, A]]
[[Category: Scislowski, L]]
[[Category: Knyphausen, P]]
[[Category: Neundorf, I]]
[[Category: De Boor, S]]
[[Category: Baumann, U]]
[[Category: Schacherl, M]]
[[Category: Lammers, M]]