4uel - Revision history

OCA at 08:20, 22 March 2023

OCA — Wed, 22 Mar 2023 08:20:38 GMT

←Older revision		Revision as of 08:20, 22 March 2023
Line 3:		Line 3:
	<StructureSection load='4uel' size='340' side='right'caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4uel' size='340' side='right'caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uel]] 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=4UEL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4UEL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uel]] 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=4UEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UEL FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</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=4uel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uel OCA], [https://pdbe.org/4uel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uel RCSB], [https://www.ebi.ac.uk/pdbsum/4uel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uel 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/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4uel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uel OCA], [~~http~~://pdbe.org/4uel PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4uel RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4uel PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4uel ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UCHL5_HUMAN UCHL5_HUMAN]] Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.<ref>PMID:16906146</ref> <ref>PMID:18922472</ref> [[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[https://www.uniprot.org/uniprot/UCHL5_HUMAN UCHL5_HUMAN] Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.<ref>PMID:16906146</ref> <ref>PMID:18922472</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[Thioesterase\|Thioesterase]]	+	*[[Thioesterase 3D structures\|Thioesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitinyl hydrolase 1]]~~	+	[[Category: Ekkebus R]]
-	~~[[Category: Dijk, W J.Van]]~~	+	[[Category: El Oualid F]]
-	[[Category: Ekkebus, R]]	+	[[Category: Ovaa H]]
-	[[Category: Oualid, F El]]	+	[[Category: Sahtoe DD]]
-	[[Category: Ovaa, H]]	+	[[Category: Sixma TK]]
-	[[Category: Sahtoe~~, D D~~]]	+	[[Category: Van Dijk WJ]]
-	[[Category: Sixma~~, T K~~]]	+
-	[[Category: ~~Adrm1]]~~	+
-	~~[[Category: Deubad]]~~	+
-	~~[[Category: Deubiquitinating enzyme]]~~	+
-	~~[[Category: Dub]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Proteasome]]~~	+
-	~~[[Category: Rpn13]]~~	+
-	~~[[Category: Ubiquitin-propargyl]]~~	+
-	~~[[Category: Uch]]~~	+
-	~~[[Category: Uch37]]~~	+
-	~~[[Category: Uchl5~~]]	+

OCA at 07:49, 3 April 2019

OCA — Wed, 03 Apr 2019 07:49:47 GMT

←Older revision		Revision as of 07:49, 3 April 2019
Line 1:		Line 1:

	==UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain==		==UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain==
-	<StructureSection load='4uel' size='340' side='right' caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4uel' size='340' side='right'caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uel]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uel]] 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=4UEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEL FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</td></tr>
Line 27:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Dijk, W J.Van]]		[[Category: Dijk, W J.Van]]

OCA at 01:13, 19 January 2017

OCA — Thu, 19 Jan 2017 01:13:46 GMT

←Older revision		Revision as of 01:13, 19 January 2017
Line 1:		Line 1:
		+
	==UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain==		==UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain==
	<StructureSection load='4uel' size='340' side='right' caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4uel' size='340' side='right' caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4uel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uel RCSB], [http://www.ebi.ac.uk/pdbsum/4uel 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=4uel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uel OCA], [http://pdbe.org/4uel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uel RCSB], [http://www.ebi.ac.uk/pdbsum/4uel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uel 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 4uel" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioesterase\|Thioesterase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:26, 4 March 2015

OCA — Wed, 04 Mar 2015 11:26:43 GMT

←Older revision		Revision as of 11:26, 4 March 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain==
		+	<StructureSection load='4uel' size='340' side='right' caption='[[4uel]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4uel]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEL FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4uem\|4uem]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4uel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uel RCSB], [http://www.ebi.ac.uk/pdbsum/4uel PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UCHL5_HUMAN UCHL5_HUMAN]] Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.<ref>PMID:16906146</ref> <ref>PMID:18922472</ref> [[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Deubiquitinating enzymes (DUBs) control vital processes in eukaryotes by hydrolyzing ubiquitin adducts. Their activities are tightly regulated, but the mechanisms remain elusive. In particular, the DUB UCH-L5 can be either activated or inhibited by conserved regulatory proteins RPN13 and INO80G, respectively. Here we show how the DEUBAD domain in RPN13 activates UCH-L5 by positioning its C-terminal ULD domain and crossover loop to promote substrate binding and catalysis. The related DEUBAD domain in INO80G inhibits UCH-L5 by exploiting similar structural elements in UCH-L5 to promote a radically different conformation, and employs molecular mimicry to block ubiquitin docking. In this process, large conformational changes create small but highly specific interfaces that mediate activity modulation of UCH-L5 by altering the affinity for substrates. Our results establish how related domains can exploit enzyme conformational plasticity to allosterically regulate DUB activity. These allosteric sites may present novel insights for pharmaceutical intervention in DUB activity.

-	~~The entry 4uel is ON HOLD until Paper Publication~~	+	Mechanism of UCH-L5 Activation and Inhibition by DEUBAD Domains in RPN13 and INO80G.,Sahtoe DD, van Dijk WJ, El Oualid F, Ekkebus R, Ovaa H, Sixma TK Mol Cell. 2015 Feb 17. pii: S1097-2765(14)01017-X. doi:, 10.1016/j.molcel.2014.12.039. PMID:25702870<ref>PMID:25702870</ref>

-	~~Authors: Sahtoe~~, D.D.~~, Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
-	[[Category: ~~El Oualid, F~~]]	+	__TOC__
-	[[Category: ~~Van~~ Dijk, W.J]]	+	</StructureSection>
-	~~[[Category: Sahtoe, D~~.~~D]]~~	+	[[Category: Ubiquitinyl hydrolase 1]]
-	~~[[Category: Sixma, T.K~~]]	+	[[Category: Dijk, W J.Van]]
	[[Category: Ekkebus, R]]		[[Category: Ekkebus, R]]
		+	[[Category: Oualid, F El]]
	[[Category: Ovaa, H]]		[[Category: Ovaa, H]]
		+	[[Category: Sahtoe, D D]]
		+	[[Category: Sixma, T K]]
		+	[[Category: Adrm1]]
		+	[[Category: Deubad]]
		+	[[Category: Deubiquitinating enzyme]]
		+	[[Category: Dub]]
		+	[[Category: Hydrolase]]
		+	[[Category: Proteasome]]
		+	[[Category: Rpn13]]
		+	[[Category: Ubiquitin-propargyl]]
		+	[[Category: Uch]]
		+	[[Category: Uch37]]
		+	[[Category: Uchl5]]

OCA at 14:16, 7 January 2015

OCA — Wed, 07 Jan 2015 14:16:32 GMT

←Older revision		Revision as of 14:16, 7 January 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4uel is ON HOLD	+	The entry 4uel is ON HOLD until Paper Publication

	Authors: Sahtoe, D.D., Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K.		Authors: Sahtoe, D.D., Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K.

OCA at 18:29, 24 December 2014

OCA — Wed, 24 Dec 2014 18:29:37 GMT

←Older revision		Revision as of 18:29, 24 December 2014
Line 6:		Line 6:

	Description: UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain		Description: UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain
		+	[[Category: Unreleased Structures]]
		+	[[Category: El Oualid, F]]
		+	[[Category: Van Dijk, W.J]]
		+	[[Category: Sahtoe, D.D]]
		+	[[Category: Sixma, T.K]]
		+	[[Category: Ekkebus, R]]
		+	[[Category: Ovaa, H]]

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

OCA — Wed, 24 Dec 2014 09:41:21 GMT

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

←Older revision

Revision as of 09:41, 24 December 2014

OCA: New page: '''Unreleased structure''' The entry 4uel is ON HOLD Authors: Sahtoe, D.D., Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K. Description: UCH-L5 in complex with ubiqui...

OCA — Wed, 24 Dec 2014 09:41:19 GMT

New page: '''Unreleased structure''' The entry 4uel is ON HOLD Authors: Sahtoe, D.D., Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K. Description: UCH-L5 in complex with ubiqui...

New page

'''Unreleased structure'''

The entry 4uel is ON HOLD

Authors: Sahtoe, D.D., Van Dijk, W.J., El Oualid, F., Ekkebus, R., Ovaa, H., Sixma, T.K.

Description: UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain