1fdz

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==N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION==
==N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION==
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<StructureSection load='1fdz' size='340' side='right' caption='[[1fdz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='1fdz' size='340' side='right'caption='[[1fdz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1fdz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FDZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1fdz]] is a 4 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=1FDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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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]] 2.6&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdz OCA], [http://pdbe.org/1fdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fdz RCSB], [http://www.ebi.ac.uk/pdbsum/1fdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdz ProSAT]</span></td></tr>
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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=1fdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdz OCA], [https://pdbe.org/1fdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdz RCSB], [https://www.ebi.ac.uk/pdbsum/1fdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237]
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[https://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fdz_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fdz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 1fdz" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1fdz" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: N-acetylneuraminate lyase]]
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[[Category: Escherichia coli]]
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[[Category: Barbosa, J A.R G]]
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[[Category: Large Structures]]
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[[Category: Hall, N E]]
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[[Category: Barbosa JARG]]
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[[Category: Lawrence, M C]]
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[[Category: Hall NE]]
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[[Category: Marcuccio, S M]]
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[[Category: Lawrence MC]]
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[[Category: Ooi, H C]]
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[[Category: Marcuccio SM]]
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[[Category: Pilling, P A]]
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[[Category: Ooi HC]]
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[[Category: Smith, B J]]
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[[Category: Pilling PA]]
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[[Category: Aldolase]]
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[[Category: Smith BJ]]
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[[Category: Alpha-keto-acid lyase]]
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[[Category: Carbon-carbon lyase]]
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[[Category: Lyase]]
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[[Category: Oxo-acid lyase]]
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Current revision

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION

PDB ID 1fdz

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