2z7g - Revision history

OCA at 13:24, 1 November 2023

OCA — Wed, 01 Nov 2023 13:24:21 GMT

←Older revision		Revision as of 13:24, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='2z7g' size='340' side='right'caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>		<StructureSection load='2z7g' size='340' side='right'caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</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]] 2.52Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [~~http~~://pdbe.org/2z7g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g 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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [https://pdbe.org/2z7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [https://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN]] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).	+	[https://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kinoshita, T]]	+	[[Category: Kinoshita T]]
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nucleotide metabolism]]~~	+
-	~~[[Category: Pharmaceutical]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Protein-inhibitor complex~~]]	+

OCA at 11:59, 29 July 2020

OCA — Wed, 29 Jul 2020 11:59:17 GMT

←Older revision		Revision as of 11:59, 29 July 2020
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	==Crystal structure of adenosine deaminase ligated with EHNA==		==Crystal structure of adenosine deaminase ligated with EHNA==
-	<StructureSection load='2z7g' size='340' side='right' caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>	+	<StructureSection load='2z7g' size='340' side='right'caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</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=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://pdbe.org/2z7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g 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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://pdbe.org/2z7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Adenosine deaminase\|Adenosine deaminase]]	+	*[[Adenosine deaminase 3D structures\|Adenosine deaminase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
		+	[[Category: Large Structures]]
	[[Category: Kinoshita, T]]		[[Category: Kinoshita, T]]
	[[Category: Acetylation]]		[[Category: Acetylation]]

OCA at 08:58, 17 October 2018

OCA — Wed, 17 Oct 2018 08:58:52 GMT

←Older revision		Revision as of 08:58, 17 October 2018
Line 1:		Line 1:
		+
	==Crystal structure of adenosine deaminase ligated with EHNA==		==Crystal structure of adenosine deaminase ligated with EHNA==
	<StructureSection load='2z7g' size='340' side='right' caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>		<StructureSection load='2z7g' size='340' side='right' caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</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=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://pdbe.org/2z7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g 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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://pdbe.org/2z7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/2z7g_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/2z7g_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 38:		Line 39:
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Kinoshita, T]]		[[Category: Kinoshita, T]]
		+	[[Category: Acetylation]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Nucleotide metabolism]]		[[Category: Nucleotide metabolism]]
		+	[[Category: Pharmaceutical]]
		+	[[Category: Polymorphism]]
	[[Category: Protein-inhibitor complex]]		[[Category: Protein-inhibitor complex]]

OCA at 21:30, 8 February 2016

OCA — Mon, 08 Feb 2016 21:30:34 GMT

←Older revision		Revision as of 21:30, 8 February 2016
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</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=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g 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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://pdbe.org/2z7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z7g ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 27:
	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 2z7g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 02:16, 25 December 2014

OCA — Thu, 25 Dec 2014 02:16:46 GMT

←Older revision		Revision as of 02:16, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>		<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g 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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN]] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Kinoshita, T.]]	+	[[Category: Kinoshita, T]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Nucleotide metabolism]]		[[Category: Nucleotide metabolism]]
	[[Category: Protein-inhibitor complex]]		[[Category: Protein-inhibitor complex]]

OCA at 05:21, 2 October 2014

OCA — Thu, 02 Oct 2014 05:21:58 GMT

←Older revision		Revision as of 05:21, 2 October 2014
Line 1:		Line 1:
-	[[~~Image~~:2z7g.~~png\|left~~\|200px]]	+	==Crystal structure of adenosine deaminase ligated with EHNA==
		+	<StructureSection load='2z7g' size='340' side='right' caption='[[2z7g]], [[Resolution\|resolution]] 2.52Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] </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=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [http://www.ebi.ac.uk/pdbsum/2z7g PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/2z7g_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Adenosine deaminase (ADA) perpetuates chronic inflammation by degrading extracellular adenosine which is toxic for lymphocytes. ADA has two distinct conformations: open form and closed form. From the crystal structures with various ligands, the non-nucleoside type inhibitors bind to the active site occupying the critical water-binding-position and sustain the open form of apo-ADA. In contrast, substrate mimics do not occupy the critical position, and induce the large conformational change to the closed form. However, it is difficult to predict the binding of (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), as it possesses characteristic parts of both the substrate and the non-nucleoside inhibitors. The crystal structure shows that EHNA binds to the open form through a novel recognition of the adenine base accompanying conformational change from the closed form of the PR-ADA complex in crystalline state.

-	~~{{STRUCTURE_2z7g\| PDB=2z7g \| SCENE= }}~~	+	Conformational change of adenosine deaminase during ligand-exchange in a crystal.,Kinoshita T, Tada T, Nakanishi I Biochem Biophys Res Commun. 2008 Aug 15;373(1):53-7. Epub 2008 Jun 10. PMID:18549808<ref>PMID:18549808</ref>

-	~~===Crystal structure~~ of ~~adenosine deaminase ligated with EHNA===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_18549808}}~~	+	==See Also==
-		+	*[[Adenosine deaminase\|Adenosine deaminase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~2z7g~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:018549808<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]

OCA: Protected "2z7g" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 22:49:12 GMT

Protected "2z7g" [edit=sysop:move=sysop]

←Older revision

Revision as of 22:49, 7 January 2013

OCA at 22:49, 7 January 2013

OCA — Mon, 07 Jan 2013 22:49:10 GMT

←Older revision		Revision as of 22:49, 7 January 2013
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-	{{Seed}}
	[[Image:2z7g.png\|left\|200px]]		[[Image:2z7g.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2z7g\| PDB=2z7g \| SCENE= }}		{{STRUCTURE_2z7g\| PDB=2z7g \| SCENE= }}

	===Crystal structure of adenosine deaminase ligated with EHNA===		===Crystal structure of adenosine deaminase ligated with EHNA===

-
-	<!--
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	{{ABSTRACT_PUBMED_18549808}}		{{ABSTRACT_PUBMED_18549808}}

	==About this Structure==		==About this Structure==
-	~~2Z7G~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA].	+	[[2z7g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18549808~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018549808</ref><references group="xtra"/>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Kinoshita, T.]]		[[Category: Kinoshita, T.]]
-	[[Category: Acetylation]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Nucleotide metabolism]]		[[Category: Nucleotide metabolism]]
-	[[Category: Pharmaceutical]]
-	[[Category: Polymorphism]]
	[[Category: Protein-inhibitor complex]]		[[Category: Protein-inhibitor complex]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:38:07 2009''

OCA at 01:38, 17 February 2009

OCA — Tue, 17 Feb 2009 01:38:09 GMT

←Older revision		Revision as of 01:38, 17 February 2009
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	==About this Structure==		==About this Structure==
-	2Z7G is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA].	+	2Z7G is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z7G OCA].

	==Reference==		==Reference==
-	~~Conformational change of adenosine deaminase during ligand-exchange in a crystal., Kinoshita T, Tada T, Nakanishi I, Biochem Biophys Res Commun. 2008 Aug 15;373(1):53-7. Epub 2008 Jun 10.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18549808 18549808]~~	+	<ref group="xtra">PMID:18549808</ref><references group="xtra"/>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Single protein]]
	[[Category: Kinoshita, T.]]		[[Category: Kinoshita, T.]]
	[[Category: Acetylation]]		[[Category: Acetylation]]
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	[[Category: Protein-inhibitor complex]]		[[Category: Protein-inhibitor complex]]

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OCA at 05:55, 16 July 2008

OCA — Wed, 16 Jul 2008 05:55:24 GMT

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