1b5p: Difference between revisions

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 ==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1==
-<StructureSection load='1b5p' size='340' side='right' caption='[[1b5p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1b5p' size='340' side='right'caption='[[1b5p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1b5p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B5P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1b5p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5P FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><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]] 1.8&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b5p RCSB], [http://www.ebi.ac.uk/pdbsum/1b5p PDBsum]</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=1b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5p OCA], [https://pdbe.org/1b5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5p RCSB], [https://www.ebi.ac.uk/pdbsum/1b5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5p ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AAPAT_THET8 AAPAT_THET8] Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).<ref>PMID:25070637</ref> <ref>PMID:30771275</ref> <ref>PMID:8907187</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/b5/1b5p_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/1b5p_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].
+</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=1b5p ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1b5p" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
+*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aspartate transaminase]]
+[[Category: Large Structures]]
-[[Category: Thermus thermophilus]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: Hirotsu, K.]]
+[[Category: Hirotsu K]]
-[[Category: Kawaguchi, S I.]]
+[[Category: Kawaguchi SI]]
-[[Category: Kuramitsu, S.]]
+[[Category: Kuramitsu S]]
-[[Category: Miyahara, I.]]
+[[Category: Miyahara I]]
-[[Category: Nakai, T.]]
+[[Category: Nakai T]]
-[[Category: Ura, H.]]
+[[Category: Ura H]]
-[[Category: Aminotransferase]]
-[[Category: Pyridoxal enzyme]]
-[[Category: Transferase]]