The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of Histidinol-phosphate aminotransferase (EC (Imidazole acetol-phosphate transferase) (tm1040) from Thermotoga maritima at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 2f8j Target Id 359801
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1436,TM1040, 3.40.640.10, 396399 Molecular Weight 39295.93 Da.
    Residues 335 Isoelectric Point 5.38
    Sequence mnpldliakraypyetekrdktylalnenpfpfpedlvdevfrrlnsdalriyydspdeeliekilsyl dtdflsknnvsvgngadeiiyvmmlmfdrsvffpptyscyrifakavgakflevpltkdlripevnvge gdvvfipnpnnptghvfereeierilktgafvaldeayyefhgesyvdflkkyenlavirtfskafsla aqrvgyvvasekfidaynrvrlpfnvsyvsqmfakvaldhreifeertkfiveerermksalremgyri tdsrgnfvfvfmekeekerllehlrtknvavrsfregvritigkreendmilrelevfk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 2.40 Rfree 0.238
    Matthews' coefficent 2.40 Rfactor 0.182
    Waters 339 Solvent Content 48.32

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    Ligand Information


    Google Scholar output for 2f8j
    1. Microbial drug target identification using different computational approaches: Specific application to Pseudomonas aeruginosa
    D Perumal, CS Lim - Innovations in Information , 2008 - ieeexplore.ieee.org

    Protein Summary

    The gene TM1040 from Thermotoga maritima encodes an enzyme histidinol-phosphate aminotransferase (HspAT), a member of aminotransferase class I and II family PF00155.  The enzyme belongs to the class of alpha and beta (a+b) proteins and reveals Pyridoxal 5′-phosphate (PLP)-dependent transferase-like fold type SCOP53382. In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes the transfer of the amino group from glutamate to imidazole acetol-phosphate producing 2-oxoglutarate and histidinol phosphate.  The structure of this enzyme from the same organism has been determined previously 1H1C. HspAT exists as a dimer.

    Ligand Summary

    Pyridoxal 5′-phosphate (PLP) is a cofactor for HspAT. PLP is covalently bound to Lys202 and accepts the amino group from L-glutamate to form the intermediate species pyridoxamine 5′-phosphate (PMP). HspAT can be purified as a mixture of PLP and PMP complex. Both forms are present in at least one copy of the active site, PMP being dominant in the other three.





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