2ada - Revision history

OCA at 09:12, 14 February 2024

2024-02-14T09:12:46Z

← Older revision		Revision as of 09:12, 14 February 2024
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	<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HPR:6~~-~~HYDROXY-7~~,~~8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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]] 2.4Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https:~~/~~/en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase]~~, ~~with EC number [https~~:~~//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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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'>[https://proteopedia.org/fgij/fg.htm?mol=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [https://pdbe.org/2ada PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [https://www.ebi.ac.uk/pdbsum/2ada PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada 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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [https://pdbe.org/2ada PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [https://www.ebi.ac.uk/pdbsum/2ada PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE]] 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_MOUSE ADA_MOUSE] 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]]
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	</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=2ada 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=2ada ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end wherein the inhibitor and a zinc are bound and completely sequestered. The presence of the zinc cofactor and the precise structure of the bound analog were not previously known. The 6R isomer of the analog is very tightly held in place by the coordination of the 6-hydroxyl to the zinc and the formation of nine hydrogen bonds. On the basis of the structure of the complex a stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles. A molecular explanation of a hereditary disease caused by several point mutations of an enzyme is also presented.

	Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.,Wilson DK, Rudolph FB, Quiocho FA Science. 1991 May 31;252(5010):1278-84. PMID:1925539<ref>PMID:1925539</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2ada" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Adenosine deaminase 3D structures\|Adenosine deaminase 3D structures]]		*[[Adenosine deaminase 3D structures\|Adenosine deaminase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Adenosine deaminase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Quiocho~~, F A~~]]		[[Category: Quiocho FA]]
	[[Category: Wilson~~, D K]]~~		[[Category: Wilson DK]]
	~~[[Category: Amino]]~~
	~~[[Category: Beta/alpha barrel]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Transition-state inhibitor]]~~
	~~[[Category: Zinc cofactor~~]]

OCA at 14:39, 17 November 2021

2021-11-17T14:39:37Z

← Older revision		Revision as of 14:39, 17 November 2021
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	<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ADA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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'>[https://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [https://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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [~~http~~://pdbe.org/2ada PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ada PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada 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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [https://pdbe.org/2ada PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [https://www.ebi.ac.uk/pdbsum/2ada PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE]] 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_MOUSE ADA_MOUSE]] 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]]

OCA at 05:01, 13 February 2020

2020-02-13T05:01:44Z

← Older revision		Revision as of 05:01, 13 February 2020
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	==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==		==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==
	<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2ada' size='340' side='right'caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
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	==See Also==		==See Also==
	*[[Adenosine deaminase\|Adenosine deaminase]]		*[[Adenosine deaminase 3D structures\|Adenosine deaminase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Quiocho, F A]]		[[Category: Quiocho, F A]]

OCA at 06:50, 9 May 2018

2018-05-09T06:50:42Z

← Older revision		Revision as of 06:50, 9 May 2018
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	==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==		==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==
	<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://pdbe.org/2ada PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada 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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://pdbe.org/2ada PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ada ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2ada_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2ada_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>

OCA at 03:52, 8 February 2016

2016-02-08T03:52:10Z

← Older revision		Revision as of 03:52, 8 February 2016
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=2ada ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:35, 10 September 2015

2015-09-10T07:35:49Z

← Older revision		Revision as of 07:35, 10 September 2015
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	<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada 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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://pdbe.org/2ada PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 2ada" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Quiocho, F A]]		[[Category: Quiocho, F A]]
	[[Category: Wilson, D K]]		[[Category: Wilson, D K]]

OCA at 20:23, 24 December 2014

2014-12-24T20:23:05Z

← Older revision		Revision as of 20:23, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada 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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE]] 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: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Quiocho, F A.]]		[[Category: Quiocho, F A]]
	[[Category: Wilson, D K.]]		[[Category: Wilson, D K]]
	[[Category: Amino]]		[[Category: Amino]]
	[[Category: Beta/alpha barrel]]		[[Category: Beta/alpha barrel]]

OCA at 00:46, 30 September 2014

2014-09-30T00:46:28Z

← Older revision		Revision as of 00:46, 30 September 2014
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	[[Image:~~2ada~~.~~png~~\|~~left~~\|~~200px~~]]		==ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS==
			<StructureSection load='2ada' size='340' side='right' caption='[[2ada]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADA FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPR:6-HYDROXY-7,8-DIHYDRO+PURINE+NUCLEOSIDE'>HPR</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=2ada FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ada OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ada RCSB], [http://www.ebi.ac.uk/pdbsum/2ada 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/ad/2ada_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 ==
			The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end wherein the inhibitor and a zinc are bound and completely sequestered. The presence of the zinc cofactor and the precise structure of the bound analog were not previously known. The 6R isomer of the analog is very tightly held in place by the coordination of the 6-hydroxyl to the zinc and the formation of nine hydrogen bonds. On the basis of the structure of the complex a stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles. A molecular explanation of a hereditary disease caused by several point mutations of an enzyme is also presented.

	~~{{STRUCTURE_2ada\| PDB=2ada \| SCENE= }}~~		Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.,Wilson DK, Rudolph FB, Quiocho FA Science. 1991 May 31;252(5010):1278-84. PMID:1925539<ref>PMID:1925539</ref>

	~~===ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_1925539}}~~		==See Also==
			*[[Adenosine deaminase\|Adenosine deaminase]]
	==~~About this Structure~~==		== References ==
	[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:001925539<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

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

2013-01-06T10:06:44Z

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

← Older revision	Revision as of 10:06, 6 January 2013
(No difference)

OCA at 10:06, 6 January 2013

2013-01-06T10:06:42Z

← Older revision		Revision as of 10:06, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2ada.png\|left\|200px]]		[[Image:2ada.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2ada", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2ada\| PDB=2ada \| SCENE= }}		{{STRUCTURE_2ada\| PDB=2ada \| SCENE= }}

	===ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS===		===ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_1925539}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 1925539 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_1925539}}		{{ABSTRACT_PUBMED_1925539}}

	==About this Structure==		==About this Structure==
	~~2ADA~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA].		[[2ada]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ada 1ada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADA OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~1925539~~</ref><references group="xtra"/>		<ref group="xtra">PMID:001925539</ref><references group="xtra"/>
	[[Category: Adenosine deaminase]]		[[Category: Adenosine deaminase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Quiocho, F A.]]		[[Category: Quiocho, F A.]]
	[[Category: Wilson, D K.]]		[[Category: Wilson, D K.]]
			[[Category: Amino]]
	~~''Page seeded by~~ [~~http~~:/~~/oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 18~~:36:~~42 2009''~~		[[Category: Beta/alpha barrel]]
			[[Category: Hydrolase]]
			[[Category: Transition-state inhibitor]]
			[[Category: Zinc cofactor]]