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1vq1

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

    Title Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution. To be published
    Site JCSG
    PDB Id 1vq1 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1209,TM0488, 84911
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.85 Rfactor 0.20824
    Waters
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    Solvent Content 56.55

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vq1
    1. Prediction of protein structure from ideal forms
    WR Taylor, GJ Bartlett, V Chelliah - Proteins: Structure, , 2008 - Wiley Online Library
     
    2. Functional site prediction selects correct protein models
    V Chelliah, WR Taylor - BMC bioinformatics, 2008 - biomedcentral.com
     
    3. Helix_sheet packing in proteins
    C Hu, P Koehl - Proteins: Structure, Function, and , 2010 - Wiley Online Library
     

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    Protein Summary

    The TM0488 gene from Thermotoga maritima encodes a N5-glutamine methyltransferase, HemK (EC 2.1.1.-)

    (PF01575, COG2890). The TM0488 structure adopts an S-adenosyl-L-methionine dependent methyltransferase fold and shows strong structural similarity (main-chain rmsd 0.4 Å over 266 residues) with N5-glutamine methyltransferase HemK from Thermotoga maritima (PDB id: 2nv8, 1sg9). See Schubert 2003 for more details on the structure and mechanism.

    Ligand Summary



    References

    Reviews

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