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<StructureSection load='1obw' size='340' side='right'caption='[[1obw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1obw' size='340' side='right'caption='[[1obw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1obw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OBW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1obw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OBW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1obw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obw OCA], [https://pdbe.org/1obw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1obw RCSB], [https://www.ebi.ac.uk/pdbsum/1obw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1obw ProSAT]</span></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=1obw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obw OCA], [https://pdbe.org/1obw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1obw RCSB], [https://www.ebi.ac.uk/pdbsum/1obw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1obw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IPYR_ECOLI IPYR_ECOLI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1obw ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1obw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown in the presence of 250 mM MgCl2. The crystal structure has been solved by Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A resolution. The upper estimate of the root-mean-square error in atomic positions is 0.26 A. These crystals belong to space group P3(2)21 with unit cell dimensions a = b = 110.27 A and c = 78.17 A. The asymmetric unit contains a trimer of subunits, i.e., half of the hexameric molecule. In the central cavity of the enzyme molecule, three Mg2+ ions, each shared by two subunits of the hexamer, are found. In the active sites of two crystallographically independent subunits, two Mg2+ ions are bound. The second active site Mg2+ ion is missing in the third subunit. A mechanism of catalysis is proposed whereby a water molecule activated by a Mg2+ ion and Tyr 55 play essential roles.
Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis.,Harutyunyan EH, Oganessyan VY, Oganessyan NN, Avaeva SM, Nazarova TI, Vorobyeva NN, Kurilova SA, Huber R, Mather T Biochemistry. 1997 Jun 24;36(25):7754-60. PMID:9201917<ref>PMID:9201917</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1obw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Inorganic diphosphatase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Avaeva, S M]]
[[Category: Avaeva SM]]
[[Category: Harutyunyan, E H]]
[[Category: Harutyunyan EH]]
[[Category: Huber, R]]
[[Category: Huber R]]
[[Category: Mather, T]]
[[Category: Mather T]]
[[Category: Oganessyan, N N]]
[[Category: Oganessyan NN]]
[[Category: Oganessyan, V Yu]]
[[Category: Oganessyan VYu]]
[[Category: Hydrolase]]
[[Category: Magnesium]]
[[Category: Metal binding]]
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