1rxd: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1rxd.gif|left|200px]]<br />
-<applet load="1rxd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rxd, resolution 1.90&Aring;" />
-'''Crystal structure of human protein tyrosine phosphatase 4A1'''<br />
-==About this Structure==
+==Crystal structure of human protein tyrosine phosphatase 4A1==
-RXD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RXD OCA].
+<StructureSection load='1rxd' size='340' side='right'caption='[[1rxd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-[[Category: Homo sapiens]]
+== Structural highlights ==
-[[Category: Single protein]]
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXD FirstGlance]. <br>
-[[Category: Almo, S.C.]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-[[Category: Burley, S.K.]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-[[Category: Fedorov, A.A.]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxd OCA], [https://pdbe.org/1rxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxd RCSB], [https://www.ebi.ac.uk/pdbsum/1rxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxd ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1rxd TOPSAN]</span></td></tr>
-[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
+</table>
-[[Category: Sun, J.P.]]
+== Evolutionary Conservation ==
-[[Category: Zhang, Z.Y.]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: new york structural genomix research consortium]]
+Check<jmol>
-[[Category: nysgxrc]]
+  <jmolCheckbox>
-[[Category: protein structure initiative]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxd_consurf.spt"</scriptWhenChecked>
-[[Category: psi]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
-[[Category: structural genomics]]
+    <text>to colour the structure by Evolutionary Conservation</text>
-[[Category: unknown function]]
+  </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/main_output.php?pdb_ID=1rxd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:08:05 2007''
+Structural genomics of protein phosphatases.,Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037<ref>PMID:18058037</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1rxd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Almo SC]]
+[[Category: Burley SK]]
+[[Category: Fedorov AA]]
+[[Category: Sun JP]]
+[[Category: Zhang ZY]]