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2nvn

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

    Title Crystal structure of hypothetical protein (YP_400729.1) from Synechococcus SP. PCC 7942 (Elongatus) at 2.50 A resolution. To be published
    Site JCSG
    PDB Id 2nvn Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1540,YP_400729.1, BIG_37, 86505
    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 5.02 Rfactor 0.208
    Waters
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    Solvent Content 75.50

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2nvn
    1. X-ray structure of Pur-_ reveals a Whirly-like fold and an unusual nucleic-acid binding surface
    A Graebsch, S Roche - Proceedings of the , 2009 - National Acad Sciences
     

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    Protein Summary

    YP_400729 (locus: Synpcc7942_1712) from Synechococcus sp. PCC 7942 (elongatus) encodes a hypothetical protein from a PFAM family PF08848 (DUF1818) with a ssDNA-binding transcriptional regulator domain fold, consisting of a repeat of two beta(4)-alpha motifs.

    YP_400729 has strong sequence and structure similarity to another JCSG solved protein, 2it9.

    STRING server reports that function of YP_400729 may be linked with its genomic neighbors: of Synpcc7942_1711, rpoZ (DNA-directed RNA polymerase omega subunit), Synpcc7942_1713 (probable hydrocarbon oxygenase MocD), and Synpcc7942_1714 (Homoserine O-acetyltransferase).

    YP_400729 has significant structural similarity to other proteins from the ssDNA fold, including MRP2 (mitochondrial RNA-binding protein 2; PDB structure 2gia) and to 2ffg, uncharacterized protein from DUF1797 family, which contains only one beta(4)-alpha motif.

    Analysis of the crystallographic packing of YP_400729 using the PQS server indicates that a dimer is the biologically relevant form.


    Ligand Summary



    References

    Reviews

    References

     

    No references found.

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