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The Open Protein Structure Annotation Network
PDB Keyword
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2q8n

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

    Title Crystal structure of Glucose-6-phosphate isomerase (EC 5.3.1.9) (TM1385) from Thermotoga maritima at 1.82 A resolution. To be published
    Site JCSG
    PDB Id 2q8n Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1281,TM1385, 3.40.50.10490, 84819
    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 3
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.91 Rfactor 0.197
    Waters
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    Solvent Content 57.70

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2q8n
    1. Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv
    K Anand, D Mathur, A Anant, LC Garg - Crystallographica Section F: , 2010 - scripts.iucr.org
     

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    Protein Summary

    G6P isomerase (PGI) is an important enzyme in glycolysis/glycogensis. It catalyzes the reversible conversion between D-GLUCOSE 6-PHOSPHATE and D-FRUCTOSE 6-PHOSPHATE. PGI is extensively studied and many structures of homolog are available. TM1385 is pretty much identical to other PGIs.

    TM1385 has a Rossmann fold with its active site formed by dimer. It is hexamer by SEC/SLS, but most other proteins are dimers though. By comparison with 1u0f, it is observed that the active site of TM1385 is very similar to 1u0f, the ligand in 1u0f can be directly copied over to fit nicely.

    Ligand Summary



    References

    Reviews

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