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    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 APC85101
    Molecular Characteristics
    Source Enterococcus faecalis v583
    Alias Ids TPS5758,AAO82176.1, PF07408, 226185 Molecular Weight 10522.35 Da.
    Residues 90 Isoelectric Point 4.74
    Sequence mdegiskkfaiqlleddaerikmlirnqknslcisqckafeevvdtqmygfsrqvtyatrlgiltndeg hrllsdlerelnqlytdvyee
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.20 Rfree 0.2436
    Matthews' coefficent 2.51 Rfactor 0.1992
    Waters 56 Solvent Content 51.09

    Ligand Information


    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

    Protein Summary

    Ligand Summary




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