4ijx: Difference between revisions

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-'''Unreleased structure'''
-The entry 4ijx is ON HOLD
+==Crystal structure of human Ap4A hydrolase E58A mutant complexed with DPO==
+<StructureSection load='4ijx' size='340' side='right'caption='[[4ijx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ijx]] is a 2 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=4IJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IJX 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4ijx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijx OCA], [https://pdbe.org/4ijx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ijx RCSB], [https://www.ebi.ac.uk/pdbsum/4ijx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ijx 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.
-Authors: Ge, H., Chen, X.
+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>
-Description: Crystal structure of human Ap4A hydrolase E58A mutant complexed with DPO
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ijx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chen X]]
+[[Category: Ge H]]