1la2

<table><tr><td colspan='2'>[[1la2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LA2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LA2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-3-phosphate_synthase Inositol-3-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.4 5.5.1.4] </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=1la2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1la2 OCA], [http://pdbe.org/1la2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1la2 RCSB], [http://www.ebi.ac.uk/pdbsum/1la2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1la2 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1la2 TOPSAN]</span></td></tr>

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== Publication Abstract from PubMed ==

The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.,Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD J Struct Funct Genomics. 2002;2(3):129-34. PMID:12836703<ref>PMID:12836703</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 1la2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Inositol-3-phosphate synthase]]

[[Category: Beckwith, A]]

[[Category: Buglino, J A]]

[[Category: Burley, S K]]

[[Category: Chadna, T]]

[[Category: Kniewel, R]]

[[Category: Lima, C D]]

[[Category: Structural genomic]]

[[Category: Shen, V]]

[[Category: Yeast]]