4o0g - Revision history

OCA at 17:05, 20 September 2023

2023-09-20T17:05:43Z

←Older revision		Revision as of 17:05, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [https://pdbe.org/4o0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [https://www.ebi.ac.uk/pdbsum/4o0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0g 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=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [https://pdbe.org/4o0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [https://www.ebi.ac.uk/pdbsum/4o0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0g ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:50, 18 January 2023

2023-01-18T08:50:02Z

←Older revision		Revision as of 08:50, 18 January 2023
Line 1:		Line 1:

	==Crystal structure of the human L-asparaginase protein T219V mutant==		==Crystal structure of the human L-asparaginase protein T219V mutant==
-	<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4o0g' size='340' side='right'caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</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=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [https://pdbe.org/4o0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [https://www.ebi.ac.uk/pdbsum/4o0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0g ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [~~http~~://pdbe.org/4o0g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o0g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ASGL1_HUMAN ASGL1_HUMAN]] Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.<ref>PMID:19839645</ref>	+	[https://www.uniprot.org/uniprot/ASGL1_HUMAN ASGL1_HUMAN] Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.<ref>PMID:19839645</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4o0g" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4o0g" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Asparaginase 3D structures\|Asparaginase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Lavie, A~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Nomme, J~~]]	+	[[Category: Lavie A]]
-	[[Category: ~~Asparaginase]]~~	+	[[Category: Nomme J]]
-	~~[[Category: Homodimer]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ntn enzyme~~]]	+

OCA at 18:32, 5 August 2016

2016-08-05T18:32:56Z

←Older revision		Revision as of 18:32, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the human L-asparaginase protein T219V mutant==		==Crystal structure of the human L-asparaginase protein T219V mutant==
	<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g 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=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://pdbe.org/4o0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0g 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 4o0g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:59, 25 December 2014

2014-12-25T20:59:44Z

←Older revision		Revision as of 20:59, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g 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=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ASGL1_HUMAN ASGL1_HUMAN]] Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.<ref>PMID:19839645</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Lavie, A.]]	+	[[Category: Lavie, A]]
-	[[Category: Nomme, J.]]	+	[[Category: Nomme, J]]
	[[Category: Asparaginase]]		[[Category: Asparaginase]]
	[[Category: Homodimer]]		[[Category: Homodimer]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Ntn enzyme]]		[[Category: Ntn enzyme]]

OCA at 06:54, 11 June 2014

2014-06-11T06:54:25Z

←Older revision		Revision as of 06:54, 11 June 2014
Line 2:		Line 2:
	<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>	+	<table><tr><td colspan='2'>[[4o0g]] is a 2 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=4O0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0G FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>		<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>
-	<tr><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat">~~<span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase]~~, ~~with EC number~~ [http://www.~~brenda-enzymes~~.~~info~~/~~php~~/~~result_flat~~.~~php4~~?~~ecno~~=~~2.7.1.2 2.7.1.2~~] ~~</span>~~</td></tr>	+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASRGL1, ALP, CRASH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span></td></tr>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Our long-term goal is the design of a human l-asparaginase (hASNase3) variant, suitable for use in cancer therapy without the immunogenicity problems associated with the currently used bacterial enzymes. Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. The key property allowing for the depletion of blood asparagine by bacterial asparaginases is their low micromolar KM value. In contrast, human enzymes have a millimolar KM for asparagine. Toward the goal of engineering an hASNase3 variant with micromolar KM, we conducted a structure/function analysis of the conserved catalytic threonine triad of this human enzyme. As a member of the N-terminal nucleophile family, to become enzymatically active, hASNase3 must undergo autocleavage between residues Gly167 and Thr168. To determine the individual contribution of each of the three conserved active-site threonines (threonine triad Thr168, Thr186, Thr219) for the enzyme-activating autocleavage and asparaginase reactions, we prepared the T168S, T186V and T219A/V mutants. These mutants were tested for their ability to cleave and to catalyze asparagine hydrolysis, in addition to being examined structurally. We also elucidated the first N-terminal nucleophile plant-type asparaginase structure in the covalent intermediate state. Our studies indicate that, while not all triad threonines are required for the cleavage reaction, all are essential for the asparaginase activity. The increased understanding of hASNase3 function resulting from these studies reveals the key regions that govern cleavage and the asparaginase reaction, which may inform the design of variants that attain a low KM for asparagine.
		+
		+	Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.,Nomme J, Su Y, Lavie A J Mol Biol. 2014 Jun 26;426(13):2471-85. doi: 10.1016/j.jmb.2014.04.016. Epub, 2014 Apr 22. PMID:24768817<ref>PMID:24768817</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Lavie, A.]]		[[Category: Lavie, A.]]
	[[Category: Nomme, J.]]		[[Category: Nomme, J.]]

OCA at 09:28, 1 May 2014

2014-05-01T09:28:58Z

←Older revision		Revision as of 09:28, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>	+	<table><tr><td colspan='2'>[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span><br>	+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span></td></tr>
		+	<table>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:01, 30 April 2014

2014-04-30T10:01:53Z

←Older revision		Revision as of 10:01, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>		[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>
-	<b>Related:</b> [[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0g RCSB], [http://www.ebi.ac.uk/pdbsum/4o0g PDBsum]</span><br>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:05, 30 April 2014

2014-04-30T08:05:55Z

←Older revision		Revision as of 08:05, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the human L-asparaginase protein T219V mutant==
-		+	<StructureSection load='4o0g' size='340' side='right' caption='[[4o0g]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~The entry~~ 4o0g is ~~ON HOLD until Apr 30 2015~~	+	== Structural highlights ==
-		+	[[4o0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0G OCA]. <br>
-	~~Authors~~: ~~Nomme~~, J., Lavie, A.	+	<b>Related:</b> [[4o0c\|4o0c]], [[4o0d\|4o0d]], [[4o0e\|4o0e]], [[4o0f\|4o0f]], [[4o0h\|4o0h]]<br>
-		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
-	~~Description~~: ~~Crystal structure of the human L-asparaginase protein T219V mutant~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Lavie, A.]]
		+	[[Category: Nomme, J.]]
		+	[[Category: Asparaginase]]
		+	[[Category: Homodimer]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ntn enzyme]]

OCA at 07:15, 23 April 2014

2014-04-23T07:15:51Z

←Older revision		Revision as of 07:15, 23 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o0g is ON HOLD until ~~Paper Publication~~	+	The entry 4o0g is ON HOLD until Apr 30 2015

	Authors: Nomme, J., Lavie, A.		Authors: Nomme, J., Lavie, A.

	Description: Crystal structure of the human L-asparaginase protein T219V mutant		Description: Crystal structure of the human L-asparaginase protein T219V mutant

OCA at 06:45, 22 January 2014

2014-01-22T06:45:24Z

←Older revision		Revision as of 06:45, 22 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o0g is ON HOLD	+	The entry 4o0g is ON HOLD until Paper Publication

	Authors: Nomme, J., Lavie, A.		Authors: Nomme, J., Lavie, A.

	Description: Crystal structure of the human L-asparaginase protein T219V mutant		Description: Crystal structure of the human L-asparaginase protein T219V mutant