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3gy1
From Proteopedia
(Difference between revisions)
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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=3gy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gy1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gy1 RCSB], [http://www.ebi.ac.uk/pdbsum/3gy1 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/3gy1 TOPSAN]</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=3gy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gy1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gy1 RCSB], [http://www.ebi.ac.uk/pdbsum/3gy1 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/3gy1 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:38, 24 December 2014
CRYSTAL STRUCTURE OF putative mandelate racemase/muconate lactonizing protein from Clostridium beijerinckii NCIMB 8052
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Categories: Clostridium beijerinckii ncimb 8052 | Almo, S C | Burley, S K | Malashkevich, V N | Morano, C | Structural genomic | Sauder, J M | Toro, R | Crystal structure | Enolase | Isomerase | Mandelate racemase/muconate lactonizing protein | NYSGXRC, New York SGX Research Center for Structural Genomics | PSI, Protein structure initiative
