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1vmd

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

    Title Crystal structure of Methylglyoxal synthase (TM1185) from Thermotoga maritima at 2.06 A resolution. To be published
    Site JCSG
    PDB Id 1vmd Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1269,TM1185, 282368
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.43 Rfactor 0.16732
    Waters
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    Solvent Content 48.93

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vmd
    1. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     

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    Protein Summary


    The gene TM1185 from Thermotoga maritima encodes an enzyme methylglyoxal synthase (MGS) COG1803.  The protein belongs to a MGS-like domain superfamily PF02142.  This domain composes the whole protein of MGS and the domain is also found in carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase.  MGS catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilize DHAP to form an ene-diolate phosphate intermediate. In MGS, the second catalytic step is characterized by the elimination of phosphate and collapse of the enediolate to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate, as in TIM. This is the first reaction in the methylglyoxal bypass of the Embden-Myerhoff glycolytic pathway and is believed to provide physiological benefits under non-ideal growth conditions in bacteria.

    Ligand Summary



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