View source for 1ihp


==STRUCTURE OF PHOSPHOMONOESTERASE==
<StructureSection load='1ihp' size='340' side='right'caption='[[1ihp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ihp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_ficuum Aspergillus ficuum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHP 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ihp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihp OCA], [https://pdbe.org/1ihp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihp RCSB], [https://www.ebi.ac.uk/pdbsum/1ihp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHYA_ASPNG PHYA_ASPNG] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
== 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/ih/1ihp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ihp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phytase is a high molecular weight acid phosphatase. The structure has an alpha/beta-domain similar to that of rat acid phosphatase and an alpha-domain with a new fold.

Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.,Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP Nat Struct Biol. 1997 Mar;4(3):185-90. PMID:9164457<ref>PMID:9164457</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ihp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phytase 3D structures|Phytase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus ficuum]]
[[Category: Large Structures]]
[[Category: Kostrewa D]]