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1vr6

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

    Title Crystal structure of Phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase) (TM0343) from Thermotoga Maritima at 1.92 A resolution. To be published
    Site JCSG
    PDB Id 1vr6 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1201,TM0343, 282169
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.20 Rfactor 0.17089
    Waters
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    Solvent Content 43.59

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vr6
    1. His-tag impact on structure
    M Carson, DH Johnson, H McDonald - Section D: Biological , 2007 - scripts.iucr.org
     
    2. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    3. Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis
    PJ Cross, RCJ Dobson, ML Patchett - Journal of Biological , 2011 - ASBMB
     
    4. An insilico approach to structural elucidation of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Arabidopsis thaliana: Hints for herbicide design
    S Bhattacharya, P Kumar - Phytochemistry, 2011 - Elsevier
     

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    Protein Summary

    The TM0343 gene from Thermotoga maritima encodes a phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase) (PF00793, COG2876, EC 2.5.1.54 ). The structure folds into a TIM beta/alpha barrel  and is essentially identical to the DAHP synthase from another hyperthermophile, Pyrococcus furiosus (PDB id: 1zco) with a main-chain rmsd ov 0.98 Å over 252 residues and a sequence identity of 62%. For more details on the structure, binding site and catalytic mechanism, see Shofield 2005.

    Ligand Summary



    References

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