1h1z

<table><tr><td colspan='2'>[[1h1z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Orysa Orysa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1Z FirstGlance]. <br>

</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h1y|1h1y]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-phosphate_3-epimerase Ribulose-phosphate 3-epimerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.1 5.1.3.1] </span></td></tr>

[[https://www.uniprot.org/uniprot/RPE1_ORYSJ RPE1_ORYSJ]] Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

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== Publication Abstract from PubMed ==

Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized after EDTA treatment and structurally elucidated by X-ray diffraction to 1.9A resolution. A prominent Zn(2+) site at the active center was established in a soaking experiment. The structure was compared with that of the EDTA-treated crystalline enzyme from the chloroplasts of potato plant leaves showing some structural differences, in particular the "closed" state of a strongly conserved mobile loop covering the substrate at its putative binding site. The previous proposal for the active center was confirmed and the most likely substrate binding position and conformation was derived from the locations of the bound zinc and sulfate ions and of three water molecules. Assuming that the bound zinc ion is an integral part of the enzyme, a reaction mechanism involving a well-stabilized cis-enediolate intermediate is suggested.

Structure and catalytic mechanism of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice.,Jelakovic S, Kopriva S, Suss KH, Schulz GE J Mol Biol. 2003 Feb 7;326(1):127-35. PMID:12547196<ref>PMID:12547196</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 1h1z" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Orysa]]

[[Category: Ribulose-phosphate 3-epimerase]]

[[Category: Jelakovic, S]]

[[Category: Schulz, G E]]

[[Category: Oxidative pentose phosphate pathway]]