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The Open Protein Structure Annotation Network
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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 283246
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1281,TM1385, 3.40.50.10490, 84819 Molecular Weight 50489.84 Da.
    Residues 448 Isoelectric Point 5.02
    Sequence mslkfdfsnlfepnisggltdedvksveekvtsavrnfventpdfakldrswidsvksledwiinfdtv vvlgiggsglgnlalhyslrplnwnemtreerngyarvfvvdnvdpdlmssvldridpkttlfnvisks gstaevmatysiargileaygldprehmlittdpekgflrklvkeegfrslevppgvggrfsvltpvgl lsamaegididelhegakdafeksmkenilenpaamialthylylnkgksisvmmaysnrmiylvdwyr qlwaeslgkrynlkgeevftgqtpvkalgatdqhsqiqlynegpndkvitflrvenfdreivipetgra elsylarkklselllaeqtgteealrennrpnmrvtfdgltpynvgqffayyeaatafmgylleinpfd qpgvelgkkitfalmgregytyeikerskkviie
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 3
    Resolution (Å) 1.82 Rfree 0.237
    Matthews' coefficent 2.91 Rfactor 0.197
    Waters 613 Solvent Content 57.70

    Pathway

    Reactions found in Metabolic Reconstruction for TM1385

    Name: glucose-6-phosphate isomerase
    Metabolic Subsystem: Glycolysis/Gluconeogenesis
    Reaction: : g6p <==> f6p
    Classification: EC:5.3.1.9
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    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
     

    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

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