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3ppl

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

    Title Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from CORYNEBACTERIUM GLUTAMICUM ATCC 13032 KITASATO at 1.25 A resolution. To be published
    Site JCSG
    PDB Id 3ppl Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS14607,NP_599493.1, 3.40.640.10, 85724
    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 2.44 Rfactor 0.1049
    Waters
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    Solvent Content 49.63

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3ppl

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    Protein Summary

     Pfam note: this protein falls into our new family Aminotran_MocR, PF12897

     

    The NP_599493 protein contains 426 residues from Corynebacterium glutamicum atcc 13032 kitasato with a calculated isoelectric point of 4.85. The crystal structural was determined at 1.30 Å resolution. Both sequence alignment and structural homolog search by Dali and SSM suggests this protein be an aspartate transaminase with conserved active site. Pyridoxal 5'-phosphate (PLP) molecules from bacterial natural processing have been indentified and modeled in the structure near Lys 259.  An unknown ligand (UNL) is bound near the PLP. The biomolecule is a dimer.

     

    390716_2.png

    Fig. 1   The monomer of protein NP_599493 complex with PLP.

     

     

    390716_1.png

    Fig. 2   The biomolecule of protein NP_599493 is a dimer.

    Ligand Summary

    Reviews

    References

     

    No references found.

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    Files (2)

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    1422.38 kB00:13, 3 Jun 2010kevinjinActions
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    1558.02 kB00:13, 3 Jun 2010kevinjinActions
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