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x * 52000, SDS-PAGE
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x * 51132, sequence calculation
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x * 78033, calculated from amino acid sequence
monomer
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
monomer
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1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
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monomer
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1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
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monomer
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1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
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additional information
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
additional information
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enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
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additional information
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enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
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additional information
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enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
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additional information
enzyme domain analysis from sequence, sequence comparisons
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
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secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
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peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons
additional information
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mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons