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The Open Protein Structure Annotation Network
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1o0x

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Proteins 56 396-400 2004
    Site JCSG
    PDB Id 1o0x Target Id 283335
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1292,TM1478 Molecular Weight 27487.50 Da.
    Residues 250 Isoelectric Point 6.62
    Sequence miriktpseiekmkkagkavavalrevrkvivpgktawdvetlvleifkklrvkpafkgyggykyatcv svneevvhglplkekvfkegdivsvdvgavyqglygdaavtyivgetdergkelvrvtrevlekaikmi kpgirlgdvshciqetvesvgfnvirdyvghgvgrelhedpqipnygtpgtgvvlrkgmtlaiepmvse gdwrvvvkedgwtavtvdgsrcahfehtilitengaeiltkeg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.254
    Matthews' coefficent 2.47 Rfactor 0.203
    Waters 195 Solvent Content 50.14

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The TM1478 gene of Thermotoga maritima encodes a methionine aminopeptidase (MAP; EC 3.4.11.18, PubMed:15211524, cd01086), that removes the ubiquitous N-terminal methionine from nascent proteins.  Methionine aminopeptidases are target proteins for the development of both anticancer and antibacterial compounds (PubMed:16420038).

    Protein encoded by TM1478 has creatinase/aminopeptidase fold (SCOP sunid:55919) with duplication composed of two very similar alpha+beta folds.


    Ligand Summary



    References

    Reviews

    References

     

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