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2gbo

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

    Title X-ray crystal structure of conserved hypothetical protein EF_2458 from Enterococcus faecalis. To be Published
    Site MCSG
    PDB Id 2gbo Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS5758,AAO82176.1, PF07408, 226185
    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 2.51 Rfactor 0.1992
    Waters
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    Solvent Content 51.09

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2gbo
    1. Identification of the Oxygen Activation Site in Monomeric Sarcosine Oxidase: Role of Lys265 in Catalysis
    G Zhao, RC Bruckner, MS Jorns - Biochemistry, 2008 - ACS Publications
     
    2. Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase
    MS Jorns, Z Chen, FS Mathews - Biochemistry, 2010 - ACS Publications
     
    3. Arginine 49 Is a Bifunctional Residue Important in Catalysis and Biosynthesis of Monomeric Sarcosine Oxidase: A Context-Sensitive Model for the Electrostatic Impact
    A Hassan-Abdallah, G Zhao, Z Chen, FS Mathews - Biochemistry, 2008 - ACS Publications
     
    4. Pleiotropic impact of a single lysine mutation on biosynthesis of and catalysis by N-methyltryptophan oxidase
    RC Bruckner, J Winans, MS Jorns - Biochemistry, 2011 - ACS Publications
     
    5. Probing Oxygen Activation Sites in Two Flavoprotein Oxidases Using Chloride as an Oxygen Surrogate
    PR Kommoju, Z Chen, RC Bruckner, FS Mathews - Biochemistry, 2011 - ACS Publications
     
    6. Covalent flavinylation of monomeric sarcosine oxidase: Identification of a residue essential for holoenzyme biosynthesis
    A Hassan-Abdallah, G Zhao, MS Jorns - Biochemistry, 2008 - ACS Publications
     

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    Protein Summary


    Ligand Summary

    Reviews

    References

     

    No references found.

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