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The Open Protein Structure Annotation Network
PDB Keyword
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3ksr

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

    Title Crystal structure of Putative serine hydrolase (NP_639225.1) from XANTHOMONAS CAMPESTRIS at 2.69 A resolution. To be Published
    Site JCSG
    PDB Id 3ksr Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS7390,NP_639225.1, 88000
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.78 Rfactor 0.197
    Waters
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    Solvent Content 55.75

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3ksr
    1. Distributed structure determination at the JCSG
    H van den Bedem, G Wolf, Q Xu - Section D: Biological , 2011 - scripts.iucr.org
     

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    Protein Summary

    Gene XCC3885 from Xanthomonas campestris encodes the NP_639225 protein belonging to the prolyl oligopeptidase group (PF00326).

    Pre-SCOP classifies 3ksr in the alpha/beta class, alpha/beta hydrolases superfamily, haloperoxidase family. Dali hits using 3ksr as query, are with 2wtn (Z=23), 1r1d, and 1tqh. Interestingly, 3ksr is similar to 2o2g (Dali Zscr=20), but it contains a novel feature: the first two strands are swapped to form a dimer. The protein is most probably a serine hydrolase based on the conservation of catalytic triad (S108/D186/H217). A PO4 ion in the active site could be relevant to function, i.e. the substrate may contain a phosphate group.

     

    Figure 1. 3ksr dimer formed by strand swapping

    dimer.png

    Figure 2. 3ksr putative active site with the catalytic triad highlighted

    FP4107a-activesite.png

    Ligand Summary

    Reviews

    References

     

    No references found.

    Tag page

    Files (2)

    FileSizeDateAttached by 
     dimer.png
    FP4107A
    147.71 kB22:50, 2 Sep 2009qxuActions
     FP4107a-activesite.png
    FP4107A active site
    211.9 kB20:31, 22 Oct 2009qxuActions
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