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The Open Protein Structure Annotation Network
PDB Keyword
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2ozg

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

    Title Crystal structure of GCN5-related N-acetyltransferase (YP_325469.1) from Anabaena variabilis ATCC 29413 at 2.00 A resolution. To be published
    Site JCSG
    PDB Id 2ozg Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1548,YP_325469.1, 103760
    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 0.161
    Waters
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    Solvent Content 47.95

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2ozg
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     

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    Protein Summary

    The Ava_4977 gene translates into the YP_325469.1 protein which belongs to the GCN5-related N-acetyl transferase (GNAT) superfamily (PF00583). This type of enzymes catalyze the transfer of the acetyl-group from acetyl-CoA to the amino group on the side chain of lysines. Its 395 amino acid long sequence carries the signature of two NAT domains (1-130 and 155-275), with the first conserved motif chelating CoA in the crystal structure (residues V84, G92, G94, I97).   

     

    SCOP divides 2ozg into two regions. Fragment 1-290 belongs to the a+b class, Acyl-Coa N-acetyl transferase superfamily, EF1021-like family. It includes both NAT domains. The second fragment (290-395) belongs to the superfamily SCP-like, EF1021 C-terminal domain-like family. The closest structures in the pdb including both fragments are 3N7Z, 2i00 and 2hv2 ; all four protein share 24-29 % sequence identity, 2ozg being the most divergent. 2ozg was also the onlt=y one that crystallized wit bound acetyl-CoA. For the N-terminal fragment, FFAS provides a -40 score with 1m44 and 1mk4, whereas FATCAT gives P-values of 3e-7 with 1vkc and 1wwz. All 4 structures are putative single NAT domains (~160 aas). Dali provides a weak match (Z-scr=16.5) with 3ddd, also a putative NAT of intermediate length (288 residues).

    Ligand Summary


    References

    Reviews

    References

     

    No references found.

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