The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain. J.Mol.Biol. 396 31-46 2010
    Site JCSG
    PDB Id 3b77 Target Id 380276
    Molecular Characteristics
    Source Exiguobacterium sibiricum 255-15
    Alias Ids TPS1752,YP_001814629.1, PF08000 Molecular Weight 22246.84 Da.
    Residues 192 Isoelectric Point 5.30
    Sequence sdigqvihpddfdkaaaddyvlhedgekiyfliksktdeycftnlalvhldgesavsskrvlyrypyah ypirhvmfetagtvdldveikfeiggkhysidvdkkqlehvkdlykallaiaekqyegqkmlefanssl nhsvtilgglrqgdmnvpqtfkdlsqesfdwlqghyykwnqkdfgsfyekyinn
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 2.42 Rfree 0.254
    Matthews' coefficent 3.07 Rfactor 0.214
    Waters 173 Solvent Content 59.98

    Ligand Information


    Google Scholar output for 3b77
    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
    2. Target domain definition and classification in CASP8
    ML Tress, I Ezkurdia - : Structure, Function, and , 2009 - Wiley Online Library
    3. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
    4. Detection and correction of underassigned rotational symmetry prior to structure deposition
    BK Poon, RW Grosse-Kunstleve, PH Zwart - Section D: Biological , 2010 - scripts.iucr.org
    5. Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain
    Q Xu, A Bateman, RD Finn, P Abdubek - Journal of molecular , 2010 - Elsevier
    6. Fold of the conserved DTC domain of deltex proteins
    J Obiero, JR Walker - : Structure, Function, and , 2012 - Wiley Online Library

    Protein Summary

    Gene Exig_2160 from Exiguobacterium sp. 255-15 encodes the YP_001814629 protein that contains two domains belonging: the conserved N-terminal PH domain  to PF08000, and the oligomerization C-terminal anti-parallel helix to PF11724

    SCOP classifies the PH domain of 3b77 inside the all-beta class, PH domain superfamily, BPHL domain family. According to DALI, 3b77 PH-domain is structurally similar to those PH domains in 3hsa, 3dcx , 1lw3, and 1kz7 (Z=10-8).

    This protein contains a conserved PH domain (40-130). Conserved domain colored red below:

    12 monomers form a pretty dodecamer that is similar to a dome-shaped cap. Conserved residues are mostly located on the PH domain. Although the function of the protein is unknown, it is possible that the sites of interest are located at the bottom of ring formed by  the PH domains. 

    Sequence conservation (14 full length homologs):

    Electrostatic surface seems to correlate well with conserved surface on PH domain ring

    Does this protein bind to other protein for its function (i.e. may not an enzyme itself)? More work is needed to figure out functional clue. Based on gene neighborhood analysis, it is possible that this protein is involved in prespore regulatory pathways in Bacillus subtilis.

    Ligand Summary





    No references found.

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