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2fea

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

    Title Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 A resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate. Proteins 69 433-439 2007
    Site JCSG
    PDB Id 2fea Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1415,2633731
    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 2.42 Rfactor 0.16
    Waters
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    Solvent Content 48.80

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2fea
    1. Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2_hydroxy_3_
    Q Xu, KS Saikatendu, S Krishna - Proteins: Structure, , 2007 - Wiley Online Library
     

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    Protein Summary

    YkrX (MtnX) encodes 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (EC 3.1.3.-) from methionine salvage pathway that produces 1,2-dihydroxy-3-keto-5-methylthiopentene.

    MtnX and MtnV are dispensable in methionine salvage pathway (PubMed:12022921). In B. subtilis mtnW (ykrW) encod enolase and mtnX (ykrX) encode phosphatase creating 1,2-dihydroxy-3-keto-5-methylthiopentene, while in other organisms, this step is performed by an enolase-phosphatase, encoded by gene mtnC, while mtnD (ykrZ) codes for the aci-reductone dioxygenase. (PubMed:15102328)

    YkrX (MtnX) has HAD-like fold (SCOP sunid:56783), with 3 layers (?/?/? parallel ?-sheet of 6 strands, order 321456). The structure of the family contains additional domain - inserted four helix bundle.


    Ligand Summary



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