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hexamer
6 * 118000, SDS-PAGE, DdPPK1 forms higher oligomeric structures in the presence of either poly phosphate or ATP
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x * 36200, about, sequence calculation
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x * 30700, about, sequence calculation
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x * 31100, about, sequence calculation
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x * 33900, about, sequence calculation
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x * 42100, about, sequence calculation
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x * 78200, about, sequence calculation
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x * 79600, about, sequence calculation
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x * 79600, about, sequence calculation
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x * 78200, about, sequence calculation
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x * 30700, about, sequence calculation
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x * 33900, about, sequence calculation
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x * 42100, about, sequence calculation
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x * 36200, about, sequence calculation
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x * 31100, about, sequence calculation
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x * 44000, SDS-PAGE, recombinant protein
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x * 44000, SDS-PAGE, recombinant protein
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x * 32000, SDS-PAGE, x * 31600, calculated from sequence
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x * 32000, SDS-PAGE, x * 31600, calculated from sequence
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x * 41000, SDS-PAGE, recombinant protein
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x * 41000, SDS-PAGE, recombinant protein
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x * 40800, deduced from nucleotide sequence
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x * 60000, denatured His-tagged protein
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x * 56419, sequence calculation, wild-type, full-length enzyme
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x * 40800, calculated from sequence
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x * 60000, denatured His-tagged protein
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x * 40800, calculated from sequence
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x * 70000, calculation from nucleotide sequence
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x * 57000, glycogen-complexed enzyme, SDS-PAGE
dimer
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homodimer
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2 * 87000, isoform PPK1, SDS-PAGE
homodimer
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x-ray crystallography
homotetramer
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4 x 39000, SDS PAGE
homotetramer
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4 x 39000, SDS PAGE
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homotetramer
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4 * 81000, gel filtration
homotetramer
x-ray crystallography
monomer
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1 * 79000, SDS-PAGE
monomer
behaves as a monomer in the absence of substrate, but addition of polyphosphate promotes dimerization
monomer
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behaves as a monomer in the absence of substrate, but addition of polyphosphate promotes dimerization
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monomer
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1 * 85000, SDS-PAGE
monomer
1 * 34750, recombinant PPK2-3, sequence calculation and SDS-PAGE
monomer
1 * 36720, recombinant PPK2-1, sequence calculation and SDS-PAGE
monomer
1 * 39950, recombinant PPK2-2, sequence calculation and SDS-PAGE
monomer
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1 * 36720, recombinant PPK2-1, sequence calculation and SDS-PAGE
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monomer
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1 * 39950, recombinant PPK2-2, sequence calculation and SDS-PAGE
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monomer
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1 * 34750, recombinant PPK2-3, sequence calculation and SDS-PAGE
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octamer
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gel filtration
octamer
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gel filtration
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octamer
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8 * 41000, in presence of P15, octamer is unstable
octamer
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8 * 41000, in presence of P15, octamer is unstable
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tetramer
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PPK2B is active as a homotetramer
tetramer
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PPK2B is active as a homotetramer
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tetramer
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4 * 69000, SDS-PAGE
tetramer
tetrameric in the crystalline state
tetramer
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tetrameric in the crystalline state
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tetramer
tetrameric in the crystalline state. Trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
tetramer
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tetrameric in the crystalline state. Trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
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tetramer
4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
tetramer
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4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
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trimer
trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
trimer
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trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
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additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
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proteome analysis of PPK motif proteins, overview
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additional information
the enzyme from Dictyostelium discoideum has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
additional information
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the enzyme from Dictyostelium discoideum has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
additional information
the structure consists of a six-stranded parallel beta-sheet surrounded by 12 alpha-helices, with a high degree of similarity to other members of the PPK2 family and the thymidylate kinase superfamily