3u53
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human Ap4A hydrolase== | |
| + | <StructureSection load='3u53' size='340' side='right'caption='[[3u53]], [[Resolution|resolution]] 2.71Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3u53]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U53 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]] 2.705Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=3u53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u53 OCA], [https://pdbe.org/3u53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u53 RCSB], [https://www.ebi.ac.uk/pdbsum/3u53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u53 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ApA hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human ApA hydrolase. Similar to the canonical Nudix fold, human ApA hydrolase shows the common alphabetaalpha-sandwich architecture. Interestingly, two sulfate ions and one diphosphate coordinated with some conserved residues were observed in the active cleft, which affords a better understanding of a possible mode of substrate binding. | ||
| - | + | Crystal structure of wild-type and mutant human Ap4A hydrolase.,Ge H, Chen X, Yang W, Niu L, Teng M Biochem Biophys Res Commun. 2013 Mar 1;432(1):16-21. doi:, 10.1016/j.bbrc.2013.01.095. Epub 2013 Feb 4. PMID:23384440<ref>PMID:23384440</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3u53" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ge HH]] | ||
| + | [[Category: Teng MK]] | ||
Current revision
Crystal structure of human Ap4A hydrolase
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