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The Open Protein Structure Annotation Network
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3gxg

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

    Title Crystal structure of Putative phosphatase (DUF442) (YP_001181608.1) from SHEWANELLA PUTREFACIENS CN-32 at 1.60 A resolution. To be published
    Site JCSG
    PDB Id 3gxg Target Id 396500
    Related PDB Ids 3gxh 
    Molecular Characteristics
    Source Shewanella putrefaciens cn-32
    Alias Ids TPS25426,YP_001181608.1, PF04273, 531944 Molecular Weight 17489.91 Da.
    Residues 156 Isoelectric Point 4.91
    Sequence niesienlqgiralqqqapqllssglpneqqfsllkqagvdvvinlmpdsskdahpdegklvtqagmdy vyipvdwqnpkvedveaffaamdqhkgkdvlvhclanyrasafaylyqlkqgqnpnmaqtmtpwndela iypkwqalltevsakygh
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.60 Rfree 0.180
    Matthews' coefficent 2.88 Rfactor 0.152
    Waters 950 Solvent Content 57.35

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3gxg
    1. S-nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration
    T Nakamura, P Cieplak, DH Cho, A Godzik, SA Lipton - Mitochondrion, 2010 - Elsevier
     
    2. Ligands in PSI structures
    A Kumar, HJ Chiu, HL Axelrod, A Morse - Section F: Structural , 2010 - scripts.iucr.org
     
    3. Ligands in crystal structures that aid in functional characterization
    AE Speers, BF Cravatt - Acta Crystallographica Section F: Structural , 2010 - scripts.iucr.org
     

    Protein Summary

    396500 is a putative novel bacteria phosphatase, representing DUF442, a subset of PFAM (PF4273 ) family of phosphotases. Its similarity to phospho-tyrosine phosphotase was noted based on sequence by A. Bateman based on sequence analysis (PUBMED id: PMC2603044). The structure of 396500 confirms that it is structurally similar to other known phosphotase, most notably, archaeal sulfolobus PTP-fold phosphatase (PDb 2i6i, rmsd 1.8 for 130 aligned Ca). A SO4 from crystallization occupies the same location of phosphoryl groups in structural homologs (near Arg130). The active site of 396500 seems noticably different from archaeal protein, suggesting a different substrate specificity or different function. In the P212121 crystal, the putative active site of one monomer is occupied by a symmetric mate.

     

    Figure 1. SO4 from crystallization solution at the location of PO4

    px6706a-site.png

    Ligand Summary

    Reviews

    References

     

    No references found.

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    Files (1)

    FileSizeDateAttached by 
     px6706a-site.png
    so4 at PO4 place
    1412.74 kB23:19, 20 Feb 2009qxuActions
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