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homodimer
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer or heterooctamer
heterooctamer
4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
heterooctamer
short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
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the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
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heterooctamer
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4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
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heterooctamer
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short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
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hexamer
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hexamer
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6 * 33367, dimers arranged in a hexamer, in the presence of AMP
hexamer
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inactive form, in complex with histidine
hexamer
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6 * 36000, viscometric methods, equilibrium centrifugation with meniscus depletion method after dialysis against 5.0 M guanidine-HCl and 0.143 M 2-mercaptoethanol
hexamer
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6 * 33000, SDS-disc gel electrophoresis
homohexamer
long enzyme form
homohexamer
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long enzyme form
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homohexamer
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer
x-ray crystallography
homohexamer
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6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
homohexamer
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6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
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homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
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the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
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homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
-
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
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octamer
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4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
octamer
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four HisGS catalytic subunits related to periplasmic binding proteins and four HisZ regulatory subunits that resemble histidyl-tRNA synthetases
octamer
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4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
additional information
quarternary structure
additional information
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quarternary structure
additional information
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overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation
additional information
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subunit structures, structure evolution