1ihp
From Proteopedia
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| - | [[Image:1ihp.jpg|left|200px]]<br /><applet load="1ihp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ihp, resolution 2.5Å" /> | ||
| - | '''STRUCTURE OF PHOSPHOMONOESTERASE'''<br /> | ||
| - | == | + | ==STRUCTURE OF PHOSPHOMONOESTERASE== |
| + | <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. | 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> | |
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| - | + | 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> | |
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| - | + | ==See Also== | |
| + | *[[Phytase 3D structures|Phytase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus ficuum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kostrewa D]] | ||
Current revision
STRUCTURE OF PHOSPHOMONOESTERASE
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