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The Open Protein Structure Annotation Network
PDB Keyword
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2obp

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

    Title Crystal structure of putative DNA-binding protein (YP_298295.1) from Ralstonia eutropha JMP134 at 1.70 A resolution. To be published
    Site JCSG
    PDB Id 2obp Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1573,YP_298295.1, 92385
    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 2.89 Rfactor 0.186
    Waters
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    Solvent Content 57.38

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2obp
    1. Enzyme adaptation to inhibitor binding: A cryptic binding site in phenylethanolamine N-methyltransferase
    CL Gee, N Drinkwater, JDA Tyndall - Journal of medicinal , 2007 - ACS Publications
     
    2. Structure of the Archaeoglobus fulgidus orphan ORF AF1382 determined by sulfur SAD from a moderately diffracting crystal
    JY Zhu, ZQ Fu, L Chen, H Xu, J Chrzas - Section D: Biological , 2012 - scripts.iucr.org
     

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    Protein Summary

    The Reut_B4095 gene from Ralstonia eutropha jmp134 encodes the YP_298295 protein, a member of the Rrf2 family of transcription regulators (e-val=0.0003) (PF02082). It has sequence similarity to the transcriptional regulator group (COG1339). The homolog gene in R. eutropha H16 strain is predicted to have a functional link by neighborhood association (score 0.87) with a transcriptional regulator of the MocR family.

    2obp structure belongs to the SCOP "winged-helix" superfamily and shows structural similarity to other transcription regulators of the same fold (e.g. DALI Z-score 12.9, rmsd 1.8 Å over 78 residues, 17% identity with PDB id: 2QVO; DALI Z-score 11.8, rmsd 2.0 Å over 73 residues, 27% identity with PDB id: 3CJN, a transcriptional regulator of the MarR family).

    Both homology and structural similarity suggest the protein may function, like MarR, as part of a resistance system.

    Ligand Summary



    References

    Reviews

    References

     

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