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The Open Protein Structure Annotation Network
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3bb9

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

    Title Crystal structure of putative ketosteroid isomerase (YP_750657.1) from Shewanella frigidimarina NCIMB 400 at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 3bb9 Target Id 378123
    Molecular Characteristics
    Source Shewanella frigidimarina ncimb 400
    Alias Ids TPS1708,YP_750657.1, 3.10.450.50, 343309 Molecular Weight 16031.33 Da.
    Residues 147 Isoelectric Point 6.28
    Sequence msagqsslsfahgdethpieqkafigvdsaagnvvkqfhaalqmgneaivrqslaanvqiyeggkvers lteyanhhmladmaylkgltitpkehqititgdiaistsishaqgeykgksidsmtmetlvlikqadgr wkithvhws
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 1.80 Rfree 0.228
    Matthews' coefficent 1.69 Rfactor 0.175
    Waters 611 Solvent Content 27.16

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3bb9
    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
     

    Protein Summary

    Gene Sfri_1973 from Shewanella frigidimarina ncimb 400  encodes a putative ketosteroid isomerase (YP_750657.1). Its genomic neighborhood is enriched in genes encoding proteins involved in copper resistance.

    The 3bb9 structure is similar to several NTF2-like proteins. Residues conserved  in 3bb9 do not superpose well with similar or identical residues of other NTF2-like proteins, but only with: the BXE_B1374 protein (PDB code 2owp; Z=14), the association domain of Ca2+/calmodulin-dependent kinase II (PDB code 1hkx; Z=14) and the ketosteroid isomerase (PDB code 1oh0; Z=13). The similarity between the clefts in 3bb9 and the ketosteroid isomerase (1oh0) indicates that both proteins might have similar function.


    Questions:
    1. What is the function of the the association domain of Ca2+/calmodulin-dependent kinase II (PF08332) present in a single domain proteins (lacking the protein kinase domain)?
    2. Is the reaction mechanism similar to that proposed by Kim et al.?

    Ligand Summary



    References

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