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The Open Protein Structure Annotation Network
PDB Keyword
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3cbu

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

    Title Crystal structure of putative glutathione S-transferase (YP_295234.1) from Ralstonia eutropha JMP134 at 2.05 A resolution. To be published
    Site JCSG
    PDB Id 3cbu Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1695,YP_295234.1, 335807
    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 3.38 Rfactor 0.171
    Waters
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    Solvent Content 63.59

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3cbu

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    Protein Summary

    Gene Reut_A1011 from Ralstonia eutropha encodes the YP_295234 protein, a probable glutathione S-transferase (GST) showing the N-terminal domain from PF02798 and the C-terminal domain from PF00043. GSTs are enzymes that inactivate toxic compounds by conjugation with glutathione and are involved in resistance towards drugs, antibiotics, insecticides and herbicides.

    pre-SCOP classifies 3cbu N-terminal domain in the alpha/beta class, thioredoxin-like superfamily, GST N-terminal domain family; and the C-terminal domain in the all alpha class, GST C-terminal domain like (super)family. DALI top hits are with GSTs like

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    (Z=29),
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    (Z=22),
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    (Z=21).

    3cbu structure forms a dimer and contains unmodeled density in the putative active site; however, it is not possible to model glutathione or one of its derivatives in the density.


    Reut_A1011 has 29% seq. id. with the GST-III from the plant Zea mays var. mutin. Like other theta-class GSTs, 3cbu contains a conserved serine residue at position 10, which is proposed to be the main catalytic residue for all theta-class GSTs.


    Ligand Summary



    References

    Reviews

    References

     

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