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3gya

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

    Title Crystal structure of putative acetyltransferase (YP_001815201.1) from EXIGUOBACTERIUM SP. 255-15 at 1.62 A resolution. To be published
    Site JCSG
    PDB Id 3gya Target Id
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    Related PDB Ids 3gy9 
    Molecular Characteristics
    Source
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    Alias Ids
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    TPS7180,YP_001815201.1, 86856
    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 2.36 Rfactor 0.179
    Waters
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    Solvent Content 47.82

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3gya

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    Protein Summary

    The fold arrangement of this structure is of minimal novelty since many (55) functionally related targets of the N-Acetyltransferases (GNAT) family have already been deposited in the Protein Data Bank (1xsn, 1ghe,3bln, 2atr, 1q2y, 2cnm, 2ob0..). The SD of these folds compared to FN12569A are in the range ~(1.8-2.3)Å. All strand blocks and a section around the bound acetyl-CoA factor (75-108) overlap well on the example of the 1ghe structure (nearest structural neighbour according to dali's Z-score). The exceptions are almost all loops, and 2 N-terminal helices (9-46). The uniqueness of the FL12569A structure is in its binding geometry of the acetyl-Co-A factor, which doesn't have any identities among all known acetyl-CoA binding molecules so far. Alone JCSG determined already 13 members of the GNAT transferases, covering wide range of species, with the highest so far resolution of 1.28A for the streptococcus 2pc1 pdb entry. The 2ogz determined by JCSG is the only GNAT member which has CoA bound and below scheme (looking from the same direction) shows the major difference in the bound ligand and the similarity of the overall fold around it : left is FL12569A right FG7303A.

     

     

     

     

     

    Ligand Summary

    Reviews

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