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The Open Protein Structure Annotation Network
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3kya

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

    Title Crystal structure of Putative phosphatase (NP_812416.1) from Bacteroides thetaiotaomicron VPI-5482 at 1.77 A resolution. To be published
    Site JCSG
    PDB Id 3kya Target Id 392960
    Molecular Characteristics
    Source Bacteroides thetaiotaomicron vpi-5482
    Alias Ids TPS20261,NP_812416.1, 332626 Molecular Weight 55604.88 Da.
    Residues 495 Isoelectric Point 4.74
    Sequence kdddnvetgafdpskpvaisdftpkeggayqklliygenfgtdvskvkvkiggkdaivinvkstyvycf vpsgafsgeieitvgegenavtttasttfsyekkmvvgtlcgyrnnrddqgwrdgpfdgpegvkccgfs dngrlafdplnkdhlyicydghkaiqlidlknrmlssplnintiptnrirsiafnkkiegyadeaeymi vaidydgkgdespsvyiikrnadgtfddrsdiqliaaykqcngatihpingelyfnsyekgqvfrldlv dyfktiknggswdpivknnpntfkqlftiadpswefqifihptgkyayfgvinnhyfmrsdydeikkef itpynfvggykqsgyrddvgtearmnnpcqgvfvknpdytgeeeydfyfvdrlnfcvrkvtpegivsty agrgastsladgnqwgtddgdlrevarfrdvsglvyddvkemfyvhdqvghtirtismeqeenvagden ipedestvesne
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.77 Rfree 0.198
    Matthews' coefficent 2.59 Rfactor 0.175
    Waters 427 Solvent Content 52.56

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The BT_3504 gene from Bacteroides thetaiotaomicron encodes a protein of unknown function. The structure contains two domains. The N-terminal domain adopts an immunoglobulin-like fold and contains an IPT/TIG signature (PF01833, residues 19-100). IPT/TIG domains are found in cell surface receptors and intracellular transcription factors. However, genome context of BT_3504 (BT_3505, putative outer membrane protein, probably involved in nutrient binding) suggests cell surface localization. The C-terminal domain adopts a 6-bladed beta-propeller fold and shows strong homology (HHPred probability 99.6%, E-value 6.5E-14, P-value 6.4E-18 over residues 140-460) to the SGL family (SMP-30/Gluconolaconase/LRE-like region, PF08450), the NHL repeat (NCL-1, HT2A and LIN-41 repeat, PF01436) and MRJP (major royal jelly protein, PF03022). In terms of structural similarity, the C-terminal domain gives the strongest hit with a calcium-dependent lactonase (PDB id: 2DG0) [Ref].

     

    See also BT_3679 (PDB id 3HRP).

     

    To do: compare ion coordination and active site residues between lactonase and BT_3504.

    1jof 3-Carboxy-cis,cis-muconate lactonizing enzyme catalytic residues HIS148 and GLU212 overlap well with GS13221D with conserved GLU334 and HIS354.

    Ligand Summary

    Reviews

    References

     

    1. (No Results)

       


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    Files (3)

    FileSizeDateAttached by 
     1jof-ACTIVEside.jpg
    GLU334 and HIS354 (yellow) overlap with catalytic resiues of 1jof 3-Carboxy-cis,cis-muconate lactonizing enzyme(red)
    344.24 kB21:38, 27 Apr 2010cbtrameActions
     SIDEgetimg.jpg
    Overall trace with ligands from side
    18.38 kB21:33, 27 Apr 2010cbtrameActions
     TOPgetimg.jpeg
    Trace es seen from TOP
    18.49 kB21:32, 27 Apr 2010cbtrameActions
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