2iuo

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[[Image:2iuo.gif|left|200px]]
 
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{{Structure
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==Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechanism of Cyanase==
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|PDB= 2iuo |SIZE=350|CAPTION= <scene name='initialview01'>2iuo</scene>, resolution 1.90&Aring;
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<StructureSection load='2iuo' size='340' side='right'caption='[[2iuo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Azi+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene>
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<table><tr><td colspan='2'>[[2iuo]] is a 10 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=2IUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUO FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cyanase Cyanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.104 4.2.1.104]
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</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>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuo OCA], [https://pdbe.org/2iuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iuo RCSB], [https://www.ebi.ac.uk/pdbsum/2iuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iuo ProSAT]</span></td></tr>
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</table>
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'''SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE'''
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== Function ==
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[https://www.uniprot.org/uniprot/CYNS_ECOLI CYNS_ECOLI] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
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== Evolutionary Conservation ==
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==About this Structure==
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[[Image:Consurf_key_small.gif|200px|right]]
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2IUO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUO OCA].
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Check<jmol>
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[[Category: Cyanase]]
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/2iuo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2iuo ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Anderson, M P.]]
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[[Category: Anderson MP]]
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[[Category: Guilloton, M.]]
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[[Category: Guilloton M]]
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[[Category: Joachimiak, A.]]
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[[Category: Joachimiak A]]
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[[Category: Walsh, M A.]]
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[[Category: Walsh MA]]
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[[Category: AZI]]
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[[Category: BR]]
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[[Category: CL]]
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[[Category: SO4]]
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[[Category: cyanate degradation]]
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[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:33:35 2008''
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Current revision

Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechanism of Cyanase

PDB ID 2iuo

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