1ami: Difference between revisions

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-{{Seed}}
-[[Image:1ami.png|left|200px]]
-<!--
+==STERIC AND CONFORMATIONAL FEATURES OF THE ACONITASE MECHANISM==
-The line below this paragraph, containing "STRUCTURE_1ami", creates the "Structure Box" on the page.
+<StructureSection load='1ami' size='340' side='right'caption='[[1ami]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ami]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AMI FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MIC:ALPHA-METHYLISOCITRIC+ACID'>MIC</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-{{STRUCTURE_1ami|  PDB=1ami  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ami FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ami OCA], [https://pdbe.org/1ami PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ami RCSB], [https://www.ebi.ac.uk/pdbsum/1ami PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ami ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACON_BOVIN ACON_BOVIN] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
+== 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/am/1ami_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=1ami ConSurf].
+<div style="clear:both"></div>
-===STERIC AND CONFORMATIONAL FEATURES OF THE ACONITASE MECHANISM===
+==See Also==
+*[[Aconitase 3D structures|Aconitase 3D structures]]
+__TOC__
-<!--
+</StructureSection>
-The line below this paragraph, {{ABSTRACT_PUBMED_7675781}}, adds the Publication Abstract to the page
-(as it appears on PubMed at http://www.pubmed.gov), where 7675781 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_7675781}}
-==About this Structure==
-AMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMI OCA].
-==Reference==
-Steric and conformational features of the aconitase mechanism., Lauble H, Stout CD, Proteins. 1995 May;22(1):1-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7675781 7675781]
-[[Category: Aconitate hydratase]]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+[[Category: Stout CD]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 20:58:59 2009''