2hu7: Difference between revisions

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 ==Binding of inhibitors by Acylaminoacyl peptidase==
-<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
+<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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]] 2.01&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hu5|2hu5]], [[2hu8|2hu8]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [https://pdbe.org/2hu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 ProSAT]</span></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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/APEH_AERPE APEH_AERPE] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.
 == 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/hu/2hu7_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2hu7_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=2hu7 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2hu7" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Acylaminoacyl peptidase|Acylaminoacyl peptidase]]
+*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Acylaminoacyl-peptidase]]
 [[Category: Aeropyrum pernix]]
-[[Category: Gengeliczki, Z.]]
+[[Category: Large Structures]]
-[[Category: Harmat, V.]]
+[[Category: Gengeliczki Z]]
-[[Category: Hornung, B.]]
+[[Category: Harmat V]]
-[[Category: Kiss, A L.]]
+[[Category: Hornung B]]
-[[Category: Polgar, L.]]
+[[Category: Kiss AL]]
-[[Category: Radi, K.]]
+[[Category: Polgar L]]
-[[Category: Sztaray, B.]]
+[[Category: Radi K]]
-[[Category: Alpha/beta hydrolase]]
+[[Category: Sztaray B]]
-[[Category: Beta-propeller]]
-[[Category: Enzyme-inhibitor complex]]
-[[Category: Hydrolase]]