4r8l - Revision history

OCA at 12:51, 1 March 2024

2024-03-01T12:51:00Z

←Older revision		Revision as of 12:51, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8L FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</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]] 2.41Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [https://pdbe.org/4r8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [https://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l 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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [https://pdbe.org/4r8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [https://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/H0W0T5_CAVPO H0W0T5_CAVPO]		[https://www.uniprot.org/uniprot/H0W0T5_CAVPO H0W0T5_CAVPO]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The initial observation that guinea pig serum kills lymphoma cells marks the serendipitous discovery of a new class of anti-cancer agents. The serum cell-killing factor was shown to be an enzyme with L-asparaginase (ASNase) activity. As a direct result of this observation, several bacterial L-asparaginases were developed and are currently FDA approved for the treatment of the subset of hematological malignancies that are dependent on the extracellular pool of the amino acid asparagine. As drugs, these enzymes act to hydrolyze asparagine to aspartate, thereby starving the cancer cells of this amino acid. Prior to the work presented here, the precise identity of this guinea pig enzyme has not been reported in the peer-reviewed literature. We discovered that the guinea pig enzyme annotated as H0W0T5_CAVPO, which we refer to as gpASNase1, has the required low Km property consistent with that possessed by the cell-killing guinea pig serum enzyme. Elucidation of the ligand-free and aspartate-complex gpASNase1 crystal structures allows a direct comparison with the bacterial enzymes and serves to explain the lack of L-glutaminase activity in the guinea pig enzyme. The structures were also used to generate a homology model for the human homolog hASNase1 and to help explain its vastly different kinetic properties compared to gpASNase1, despite a 70% sequence identity. Given that the bacterial enzymes frequently present immunogenic and other toxic side effects, this work suggests that gpASNase1 could be a promising alternative to these bacterial enzymes.
-
-	Identification and Structural Analysis of an L-asparaginase Enzyme from Guinea Pig with Putative Tumor Cell-killing Properties.,Schalk AM, Nguyen HA, Rigouin C, Lavie A J Biol Chem. 2014 Oct 15. pii: jbc.M114.609552. PMID:25320094<ref>PMID:25320094</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4r8l" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:44, 2 March 2023

2023-03-02T06:44:28Z

←Older revision		Revision as of 06:44, 2 March 2023
Line 3:		Line 3:
	<StructureSection load='4r8l' size='340' side='right'caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='4r8l' size='340' side='right'caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Cavpo Cavpo~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R8L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [https://pdbe.org/4r8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [https://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10141 CAVPO])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [~~http~~://pdbe.org/4r8l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/H0W0T5_CAVPO H0W0T5_CAVPO]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Asparaginase]]~~	+	[[Category: Cavia porcellus]]
-	~~[[Category: Cavpo~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lavie, A]]	+	[[Category: Lavie A]]
-	[[Category: Schalk~~, A M]]~~	+	[[Category: Schalk AM]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: L-asparaginase~~]]	+

OCA at 10:23, 1 May 2019

2019-05-01T10:23:54Z

←Older revision		Revision as of 10:23, 1 May 2019
Line 1:		Line 1:

	==Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain==		==Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain==
-	<StructureSection load='4r8l' size='340' side='right' caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>	+	<StructureSection load='4r8l' size='340' side='right'caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cavpo Cavpo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8L FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10141 CAVPO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://pdbe.org/4r8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l 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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://pdbe.org/4r8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l ProSAT]</span></td></tr>
Line 23:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Asparaginase]]		[[Category: Asparaginase]]
		+	[[Category: Cavpo]]
		+	[[Category: Large Structures]]
	[[Category: Lavie, A]]		[[Category: Lavie, A]]
	[[Category: Schalk, A M]]		[[Category: Schalk, A M]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: L-asparaginase]]		[[Category: L-asparaginase]]

OCA at 17:25, 18 January 2017

2017-01-18T17:25:43Z

←Older revision		Revision as of 17:25, 18 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain==		==Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain==
	<StructureSection load='4r8l' size='340' side='right' caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='4r8l' size='340' side='right' caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l 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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://pdbe.org/4r8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8l ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4r8l" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:37, 10 December 2014

2014-12-10T12:37:00Z

←Older revision		Revision as of 12:37, 10 December 2014
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Asparaginase]]		[[Category: Asparaginase]]
-	[[Category: Lavie, A.]]	+	[[Category: Lavie, A]]
-	[[Category: Schalk, A M.]]	+	[[Category: Schalk, A M]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: L-asparaginase]]		[[Category: L-asparaginase]]

OCA at 09:34, 29 October 2014

2014-10-29T09:34:36Z

←Older revision		Revision as of 09:34, 29 October 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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l 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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The initial observation that guinea pig serum kills lymphoma cells marks the serendipitous discovery of a new class of anti-cancer agents. The serum cell-killing factor was shown to be an enzyme with L-asparaginase (ASNase) activity. As a direct result of this observation, several bacterial L-asparaginases were developed and are currently FDA approved for the treatment of the subset of hematological malignancies that are dependent on the extracellular pool of the amino acid asparagine. As drugs, these enzymes act to hydrolyze asparagine to aspartate, thereby starving the cancer cells of this amino acid. Prior to the work presented here, the precise identity of this guinea pig enzyme has not been reported in the peer-reviewed literature. We discovered that the guinea pig enzyme annotated as H0W0T5_CAVPO, which we refer to as gpASNase1, has the required low Km property consistent with that possessed by the cell-killing guinea pig serum enzyme. Elucidation of the ligand-free and aspartate-complex gpASNase1 crystal structures allows a direct comparison with the bacterial enzymes and serves to explain the lack of L-glutaminase activity in the guinea pig enzyme. The structures were also used to generate a homology model for the human homolog hASNase1 and to help explain its vastly different kinetic properties compared to gpASNase1, despite a 70% sequence identity. Given that the bacterial enzymes frequently present immunogenic and other toxic side effects, this work suggests that gpASNase1 could be a promising alternative to these bacterial enzymes.
		+
		+	Identification and Structural Analysis of an L-asparaginase Enzyme from Guinea Pig with Putative Tumor Cell-killing Properties.,Schalk AM, Nguyen HA, Rigouin C, Lavie A J Biol Chem. 2014 Oct 15. pii: jbc.M114.609552. PMID:25320094<ref>PMID:25320094</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:46, 22 October 2014

2014-10-22T11:46:29Z

←Older revision		Revision as of 11:46, 22 October 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain==
-		+	<StructureSection load='4r8l' size='340' side='right' caption='[[4r8l]], [[Resolution\|resolution]] 2.41Å' scene=''>
-	~~The entry~~ 4r8l is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r8l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8L FirstGlance]. <br>
-	~~Authors~~: ~~Schalk~~, A.M., Lavie, A.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r8k\|4r8k]]</td></tr>
-	~~Description~~: ~~Crystal structure of the Asp-bound guinea pig~~ L-asparaginase ~~1 catalytic domain~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=4r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8l RCSB], [http://www.ebi.ac.uk/pdbsum/4r8l PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Asparaginase]]
		+	[[Category: Lavie, A.]]
		+	[[Category: Schalk, A M.]]
		+	[[Category: Hydrolase]]
		+	[[Category: L-asparaginase]]

OCA at 08:25, 24 September 2014

2014-09-24T08:25:39Z

←Older revision		Revision as of 08:25, 24 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r8l is ON HOLD	+	The entry 4r8l is ON HOLD until Paper Publication

	Authors: Schalk, A.M., Lavie, A.		Authors: Schalk, A.M., Lavie, A.

	Description: Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain		Description: Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain

OCA: Protected "4r8l" [edit=sysop:move=sysop]

2014-09-10T08:26:12Z

Protected "4r8l" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:26, 10 September 2014

OCA: New page: '''Unreleased structure''' The entry 4r8l is ON HOLD Authors: Schalk, A.M., Lavie, A. Description: Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain

2014-09-10T08:26:11Z

New page: '''Unreleased structure''' The entry 4r8l is ON HOLD Authors: Schalk, A.M., Lavie, A. Description: Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain

New page

'''Unreleased structure'''

The entry 4r8l is ON HOLD

Authors: Schalk, A.M., Lavie, A.

Description: Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain