The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of MYO-inositol-1-phosphate synthase-related protein (TM1419) from Thermotoga maritima at 1.70 A resolution. To be published
    Site JCSG
    PDB Id 3cin Target Id 283279
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1286,TM1419, 84803 Molecular Weight 42192.09 Da.
    Residues 382 Isoelectric Point 5.31
    Sequence mvkvlilgqgyvastfvagleklrkgeiepygvplarelpigfedikivgsydvdrakigkklsevvkq ywndvdsltsdpeirkgvhlgsvrnlpieaegledsmtlkeavdtlvkewteldpdvivntctteafvp fgnkedllkaienndkerltatqvyayaaalyankrggaafvnviptfiandpafvelakennlvvfgd dgatgatpftadvlshlaqrnryvkdvaqfniggnmdflaltddgknkskeftkssivkdilgydaphy ikptgyleplgdkkfiaihieyvsfngatdelmingrindspalggllvdlvrlgkialdrkefgtvyp vnafymknpgpaeeknipriiayekmriwaglkpkwl
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.70 Rfree 0.194
    Matthews' coefficent 2.43 Rfactor 0.160
    Waters 235 Solvent Content 49.47

    Ligand Information


    Google Scholar output for 3cin
    1. Pyridobenzothiazole derivatives as new chemotype targeting the HCV NS5B polymerase
    G Manfroni, F Meschini, ML Barreca, P Leyssen - Bioorganic & Medicinal , 2011 - Elsevier

    Protein Summary

    The gene TM1419 from Thermotoga maritima encodes the NP_229219 protein, an inositol-3-phosphate synthase EC: PF01658. Analysis by SCOP indicates that the inositol-3-phosphate synthase from Thermotoga maritima has two structural domains: N-terminal domain (1-209) belongs to the NAD(P)-binding Rossmann-fold domain superfamily, glyceraldehyde-3-phosphate dehydrogenase-like N-terminal domain family (SCOP51734); the C-terminal domain (211-316) belongs to the gyceraldehyde-3-phosphate dehydrogenase-like C-terminal domain superfamily, dihydrodipicolinate reductase-like family. According to DALI, similar structures are: 1JKI (Z=36), 1U1I (Z=41), and 1GR0 (Z=29).

    The enzyme catalyzes the conversion of D-glucose 6-phosphate to 1-L-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. Homologous sequences are distributed across all kingdoms of life, but viruses. A two-reaction pathway is found for myo-inositol biosynthesis in all eukaryotic cells. First, glucose-6-phosphate is cyclized to form myo-inositol 1-phosphate, which is then dephosphorylated in the next step to produce free myo-inositol. These two steps are catalyzed by myo-inositol 1-phosphate synthase (EC (IPS) and inositol monophosphatase (EC:, respectively [Ref].  

    Ligand Summary





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