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3s47

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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=3s47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s47 RCSB], [http://www.ebi.ac.uk/pdbsum/3s47 PDBsum]</span></td></tr>
<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=3s47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s47 RCSB], [http://www.ebi.ac.uk/pdbsum/3s47 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/A6M2W4_CLOB8 A6M2W4_CLOB8]] Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.
==See Also==
==See Also==

Revision as of 13:17, 25 December 2014

Crystal structure of enolase superfamily member from Clostridium beijerincki complexed with Mg

3s47, resolution 1.70Å

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