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{{STRUCTURE_3men|  PDB=3men  |  SCENE=  }}
===Crystal structure of acetylpolyamine aminohydrolase from Burkholderia pseudomallei, iodide soak===
{{ABSTRACT_PUBMED_21359836}}


==Function==
==Crystal structure of acetylpolyamine aminohydrolase from Burkholderia pseudomallei, iodide soak==
[[http://www.uniprot.org/uniprot/Q3JUN4_BURP1 Q3JUN4_BURP1]] Acts on many types of acetylpolyamines. Has high affinity towards acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine. Acts on L-Lys-(epsilon-acetyl)-coumarin, but has very low activity towards acetylated peptides (By similarity).  
<StructureSection load='3men' size='340' side='right'caption='[[3men]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3men]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MEN FirstGlance]. <br>
[[3men]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MEN OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3men FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3men OCA], [https://pdbe.org/3men PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3men RCSB], [https://www.ebi.ac.uk/pdbsum/3men PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3men ProSAT]</span></td></tr>
<ref group="xtra">PMID:021359836</ref><references group="xtra"/><references/>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APAHL_BURP1 APAHL_BURP1] Involved in polyamine metabolism. Catalyzes the deacetylation of various acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine.[UniProtKB:Q48935]
== 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/me/3men_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=3men ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]
[[Category: Large Structures]]
[[Category: Acetylpolyamine aminohydrolase]]
[[Category: Histone deacetylase]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/3men"