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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of a Deoxyribose-phosphate aldolase (TM_1559) from THERMOTOGA MARITIMA at 1.75 A resolution. To be published
    Site JCSG
    PDB Id 3r12 Target Id 283416
    Related PDB Ids 3r13 
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1298,TM1559, 84798 Molecular Weight 27283.87 Da.
    Residues 248 Isoelectric Point 5.24
    Sequence mieyrieeavakyrefyefkpvresagiedvksaiehtnlkpfatpddikklclearenrfhgvcvnpc yvklareelegtdvkvvtvvgfplganetrtkaheaifavesgadeidmvinvgmlkakeweyvyedir svvesvkgkvvkviietcyldteekiaacvisklagahfvktstgfgtggataedvhlmkwivgdemgv kasggirtfedavkmimygadrigtssgvkivqggeerygg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.75 Rfree 0.1915
    Matthews' coefficent 2.02 Rfactor 0.1529
    Waters 256 Solvent Content 39.03

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    Ligand Information


    Google Scholar output for 3r12

    Protein Summary

    The gene TM1559 from Thermotoga maritima encodes 2-deoxyribose-5-phosphate aldolase (DERA)  from the DeoC family of aldolase enzymes PF01791 COG0274.  This enzyme participates in the pentose phosphate pathway.  DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes.  Because of its unique enzymatic reaction and broad substrate specificity, the enzyme has become an industrial biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.  The enzyme has been optimized for numerous industrial chemistry processes using the directed evolution approach [Ref].

    Ligand Summary





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