1ihp: Difference between revisions
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New page: left|200px<br /><applet load="1ihp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihp, resolution 2.5Å" /> '''STRUCTURE OF PHOSPHOM... |
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== | ==STRUCTURE OF PHOSPHOMONOESTERASE== | ||
Phytase is a high molecular weight acid phosphatase. The structure has an | <StructureSection load='1ihp' size='340' side='right'caption='[[1ihp]], [[Resolution|resolution]] 2.50Å' 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]] 2.5Å</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®/PubMed®, 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: Aspergillus ficuum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Kostrewa | [[Category: Kostrewa D]] | ||