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The Open Protein Structure Annotation Network
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2fm1

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

    Title Crystal structure of L-ALLO-threonine aldolase (tm1744) from Thermotoga maritima at 2.25 A resolution. To be published
    Site JCSG
    PDB Id 2fm1 Target Id 283599
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1313,TM1744, 3.40.640.10, 289550 Molecular Weight 37572.08 Da.
    Residues 343 Isoelectric Point 6.23
    Sequence midlrsdtvtkpteemrkamaqaevgddvygedptinelerlaaetfgkeaalfvpsgtmgnqvsimah tqrgdevileadshifwyevgamavlsgvmphpvpgkngamdpddvrkairprnihfprtsliaienth nrsggrvvplenikeictiakehginvhidgarifnasiasgvpvkeyagyadsvmfclskglcapvgs vvvgdrdfierarkarkmlgggmrqagvlaaagiialtkmvdrlkedhenarflalklkeigysvnped vktnmvilrtdnlkvnahgfiealrnsgvlanavsdteirlvthkdvsrndieealnifeklfrkfs
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 2.25 Rfree 0.216
    Matthews' coefficent 2.21 Rfactor 0.142
    Waters 1059 Solvent Content 43.95

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2fm1
    1. The Three-dimensional Structure of N-Succinyldiaminopimelate Aminotransferase from Mycobacterium tuberculosis
    S Weyand, G Kefala, MS Weiss - Journal of molecular biology, 2007 - Elsevier
     

    Protein Summary

    The gene TM1744 from Thermotoga maritima encodes low-specificity threonine aldolase (TA).  The enzyme belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I) SCOP53384. TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.  Several crystal structures of the enzyme from the same organism are available: 1JG8, 1LW4, 1M6S.

    Ligand Summary



    References

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