5uq6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE IN TWO COORDINATION MODES ALONG WITH A BRIDGING HYDROXIDE ION== | |
| + | <StructureSection load='5uq6' size='340' side='right' caption='[[5uq6]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5uq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UQ6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5uq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uq6 OCA], [http://pdbe.org/5uq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5uq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uq6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PPA5_PIG PPA5_PIG]] Uteroferrin is a phosphoprotein phosphatase, synthesized in response to progesterone. It appears to function in transplacental transport of iron in pig. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for chemotherapeutics. Knowledge about their reaction mechanisms and associated transition states greatly aids the design of potent and highly specific drug leads. By using a high-resolution crystal structure, we have probed the trajectory of the reaction catalyzed by purple acid phosphatase, an enzyme essential for the integrity of bone structure. In particular, the transition state is visualized, thus providing detailed structural information that may be exploited in the design of specific inhibitors for the development of new anti-osteoporotic chemotherapeutics. | ||
| - | + | Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme.,Selleck C, Clayton D, Gahan LR, Mitic N, McGeary RP, Pedroso MM, Guddat LW, Schenk G Chemistry. 2017 Apr 6;23(20):4778-4781. doi: 10.1002/chem.201700866. Epub 2017, Mar 23. PMID:28261912<ref>PMID:28261912</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5uq6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acid phosphatase]] | ||
| + | [[Category: Sus scrofa]] | ||
| + | [[Category: Clayton, D]] | ||
| + | [[Category: Guddat, L]] | ||
| + | [[Category: Schenk, G]] | ||
| + | [[Category: Selleck, C]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydroxide]] | ||
| + | [[Category: Metallohydrolase]] | ||
| + | [[Category: Transition state]] | ||
Revision as of 13:39, 24 May 2017
PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE IN TWO COORDINATION MODES ALONG WITH A BRIDGING HYDROXIDE ION
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