3mvi: Difference between revisions

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 ==Crystal structure of holo mADA at 1.6 A resolution==
-<StructureSection load='3mvi' size='340' side='right' caption='[[3mvi]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='3mvi' size='340' side='right'caption='[[3mvi]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mvi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MVI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mvi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MVI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a4m|1a4m]], [[3mvt|3mvt]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ada ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3mvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvi OCA], [https://pdbe.org/3mvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mvi RCSB], [https://www.ebi.ac.uk/pdbsum/3mvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mvi ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/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=3mvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvi OCA], [http://pdbe.org/3mvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mvi RCSB], [http://www.ebi.ac.uk/pdbsum/3mvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mvi ProSAT]</span></td></tr>
 </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).
+[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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 ==See Also==
-*[[Adenosine deaminase|Adenosine deaminase]]
+*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Adenosine deaminase]]
+[[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Cera, E Di]]
+[[Category: Chen Z]]
-[[Category: Chen, Z]]
+[[Category: Di Cera E]]
-[[Category: Frieden, C]]
+[[Category: Frieden C]]
-[[Category: Mathews, S]]
+[[Category: Mathews S]]
-[[Category: Niu, W]]
+[[Category: Niu W]]
-[[Category: Shu, Q]]
+[[Category: Shu Q]]
-[[Category: Hydrolase]]