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The Open Protein Structure Annotation Network
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3lwu

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

    Title Crystal structure of Putative succinylglutamate desuccinylase/aspartoacylase (YP_749235.1) from Shewanella frigidimarina NCIMB 400 at 2.10 A resolution. To be published
    Site JCSG
    PDB Id 3lwu Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS20121,YP_749235.1, 93039
    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 3.01 Rfactor 0.160
    Waters
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    Solvent Content 59.17

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3lwu

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    Protein Summary

    The protein YP_749235.1 is annotated as Succinylglutamate desuccinylase/aspartoacylase. YP_749235.1 belongs to PFAM PF04952 AstE_AspA which includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyses the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. 

    Further information on these proteins may be found in the Topsan Zinc Peptidase  page.


    The protein has an unknown ligand (UNL) bound in the active site near Zn. The UNL resembles a derivative of Glutamate which could be related to Succinyl-Glutamate.

    HP10632F.png

    Figure 1: The monomer structure with Zn shown as a green sphere.

     HP10632F_UNL.png

    Figure 2: The active site. The Zn ion is colored magenta. The unknown ligand (UNL)  is shown in spherical and stick representation in cyan color and resembles glutamate or a derivative of succynyl-glutamate.

     

    HP10632F_tetramer.png

    Figure 3: The most probable oligomeric state based on size exclusion and crystal packing data.

     

    There are two other related proteins solved by JCSG:  3fmc and 2qj8

    Ligand Summary

    Reviews

    References

     

    No references found.

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