3dyd: Difference between revisions

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-[[Image:3dyd.png|left|200px]]
-{{STRUCTURE_3dyd|  PDB=3dyd  |  SCENE=  }}
+==Human Tyrosine Aminotransferase==
+<StructureSection load='3dyd' size='340' side='right'caption='[[3dyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3dyd]] 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=3DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=3dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyd OCA], [https://pdbe.org/3dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyd RCSB], [https://www.ebi.ac.uk/pdbsum/3dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyd ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:[https://omim.org/entry/276600 276600]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.<ref>PMID:1357662</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.<ref>PMID:7999802</ref> <ref>PMID:16640556</ref>
+== 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/dy/3dyd_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/main_output.php?pdb_ID=3dyd ConSurf].
+<div style="clear:both"></div>
-===Human Tyrosine Aminotransferase===
+==See Also==
+*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-[[3dyd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYD OCA].
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Tyrosine transaminase]]
+[[Category: Large Structures]]
-[[Category: Andersson, J.]]
+[[Category: Andersson J]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Arrowsmith CH]]
-[[Category: Berg, S Van Den.]]
+[[Category: Berglund H]]
-[[Category: Berglund, H.]]
+[[Category: Collins R]]
-[[Category: Collins, R.]]
+[[Category: Dahlgren LG]]
-[[Category: Dahlgren, L G.]]
+[[Category: Edwards AM]]
-[[Category: Edwards, A M.]]
+[[Category: Flodin S]]
-[[Category: Flodin, S.]]
+[[Category: Flores A]]
-[[Category: Flores, A.]]
+[[Category: Graslund S]]
-[[Category: Graslund, S.]]
+[[Category: Hammarstrom M]]
-[[Category: Hammarstrom, M.]]
+[[Category: Johansson A]]
-[[Category: Johansson, A.]]
+[[Category: Johansson I]]
-[[Category: Johansson, I.]]
+[[Category: Karlberg T]]
-[[Category: Karlberg, T.]]
+[[Category: Kotenyova T]]
-[[Category: Kotenyova, T.]]
+[[Category: Lehtio L]]
-[[Category: Lehtio, L.]]
+[[Category: Moche M]]
-[[Category: Moche, M.]]
+[[Category: Nilsson ME]]
-[[Category: Nilsson, M E.]]
+[[Category: Nordlund P]]
-[[Category: Nordlund, P.]]
+[[Category: Nyman T]]
-[[Category: Nyman, T.]]
+[[Category: Olesen K]]
-[[Category: Olesen, K.]]
+[[Category: Persson C]]
-[[Category: Persson, C.]]
+[[Category: Sagemark J]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Schuler H]]
-[[Category: Sagemark, J.]]
+[[Category: Thorsell AG]]
-[[Category: Schuler, H.]]
+[[Category: Tresaugues L]]
-[[Category: Thorsell, A G.]]
+[[Category: Van Den Berg S]]
-[[Category: Tresaugues, L.]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J.]]
+[[Category: Welin M]]
-[[Category: Welin, M.]]
+[[Category: Wikstrom M]]
-[[Category: Wikstrom, M.]]
+[[Category: Wisniewska M]]
-[[Category: Wisniewska, M.]]
-[[Category: Aminotransferase]]
-[[Category: Disease mutation]]
-[[Category: Phenylalanine catabolism]]
-[[Category: Plp]]
-[[Category: Pyridoxal phosphate]]
-[[Category: Sgc]]
-[[Category: Structural genomic]]
-[[Category: Structural genomics consortium]]
-[[Category: Transferase]]
-[[Category: Tyrosine]]
-[[Category: Tyrosine catabolism]]