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1vr8

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

    Title Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 A resolution reveals a fold similar to the Ran-binding protein Mog1p. Proteins 65 777-782 2006
    Site JCSG
    PDB Id 1vr8 Target Id 358480
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1395,TM1622 Molecular Weight 15125.72 Da.
    Residues 130 Isoelectric Point 8.77
    Sequence ppeaysldtaifvletrdyrlsdvkeidsygdvemkgkvavfeteygpvflyvykgeeakkiwkklngr agfvsirsvldlpnmgkfstvsngkkivawwrknwlfivegkngveefvkhvyrvyeemkq
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.75 Rfree 0.18179
    Matthews' coefficent 2.32 Rfactor 0.1486
    Waters 172 Solvent Content 46.46

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vr8
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. Insights into proteinprotein interfaces using a Bayesian network prediction method
    JR Bradford, CJ Needham, AJ Bulpitt - Journal of molecular , 2006 - Elsevier
     
    3. 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
     
    4. The structure of RseB: a sensor in periplasmic stress response of E. coli
    P Wollmann, K Zeth - Journal of molecular biology, 2007 - Elsevier
     
    5. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     
    6. Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 resolution reveals a fold similar to the Ran_binding protein Mog1p
    Q Xu, S Krishna, D McMullan - Proteins: Structure, , 2006 - Wiley Online Library
     
    7. Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634
    CJ McCleverty, L Columbus, A Kreusch - Protein , 2008 - Wiley Online Library
     
    8. Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft
    A Cavazos, DM Prigozhin, T Alber - Journal of Molecular Biology, 2012 - Elsevier
     
    9. The Structure of RseB, a Sensor for Periplasmic Stress in Escherichia coli
    P Wollmann - 2008 - edoc.ub.uni-muenchen.de
     

    Protein Summary

    Crystal structure of TM1622 from Thermotoga maritima has uniq structure and sequence. TM1622 fold resembles fold of Ran-binding protein Mog1p, but lacks a characteristic N-terminal ?-hairpin.

    PFP server identified TM1622 as"Rab GTPase binding" (GO:0017137; PubMed:16672240).

    Ligand Summary



    References

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