1ush

<table><tr><td colspan='2'>[[1ush]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1USH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ush FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ush OCA], [http://pdbe.org/1ush PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ush RCSB], [http://www.ebi.ac.uk/pdbsum/1ush PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ush ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/USHA_ECOLI USHA_ECOLI]] Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.

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== Publication Abstract from PubMed ==

The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.

X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.,Knofel T, Strater N Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872<ref>PMID:10331872</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ush" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: 5'-nucleotidase]]

[[Category: Ecoli]]

[[Category: Knofel, T]]

[[Category: Strater, N]]

[[Category: Udp-sugar hydrolase]]