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eicosamer
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20 * 50000, SDS-PAGE
pentadecamer
structure modelling of a structure consisting of three pentamers, overview
tetramer
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4 * 43000, minor peak in gel filtration with a mass of 190000 detected for both mutant enzymes
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x * 40000, about, sequence calculation
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x * 39300, recombinant His-tagged enzyme, SDS-PAGE
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x * 50000, about, SDS-PAGE
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x * 70000, fusion-protein with SUMO-tag, SDS-PAGE and calculated
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x * 40000, SDS-PAGE, x * 38759, calculated
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x * 41978, calculation from nucleotide sequence
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x * 40509, sequence calculation
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x * 51800, sedimentation equilibrium experiments in 6 M urea
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x * 50100, wild-type enzyme, SDS-PAGE, x * 79600, recombinant GST-tagged wild-type enzyme, SDS-PAGE
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x * 50100, wild-type enzyme, SDS-PAGE, x * 79600, recombinant GST-tagged wild-type enzyme, SDS-PAGE
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x * 40000, about, recombinant His6-tagged isozyme GS1beta1, SDS-PAGE, x * 39399, about, native isozyme, sequence calculation
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x * 40000, about, recombinant His6-tagged isozyme GS1gamma1, SDS-PAGE, x * 39399, about, native isozyme, sequence calculation
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x * 46691, Unigene0016999, sequence calculation, x * 55408, Unigene0017002, sequence calculation, x * 38300, Unigene0015608, sequence calculation, x * 38750, Unigene0022741, sequence calculation, x * 43909, Unigene0002184, sequence calculation, x * 83726, Unigene0002194, sequence calculation
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x * 43500, recombinant His-tagged enzyme, SDS-PAGE
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x * 43500, recombinant His-tagged enzyme, SDS-PAGE
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x * 47212, calculated, x * 42000, recombinant protein lacking the target peptide, SDS-PAGE
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x * 47000, about, full-length wild-type isozyme GS2a, sequence calculation, x * 41700, about, mature and active isozyme GS2a without transit peptide, sequence calculation, x * 40000, about, mutant isozyme GS2a with cleaved N- and C-terminal peptides, sequence calculation
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x * 45000, calculated from sequence
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x * 45000, calculated from sequence
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x * 46700, about, GlnA3, sequence calculation
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x * 49600, about, GlnA2, sequence calculation
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x * 49700, about, GlnA4, sequence calculation
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x * 53600, about, GlnA1, sequence calculation
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x * 54000, SDS-PAGE
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x * 49600, about, GlnA2, sequence calculation
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x * 53600, about, GlnA1, sequence calculation
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x * 58000, SDS-PAGE
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x * 56000, recombinant isozyme GSI
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x * 56000, recombinant isozyme GSI
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x * 53348, calculated from sequence
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x * 53348, calculated from sequence
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x * 45000, recombinant enzyme, SDS-PAGE, x * 40700, about, sequence calculation
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x * 42000, isoenzyme GS1, SDS-PAGE
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x * 45000, isoenzyme GS2, SDS-PAGE
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x * 79416, calculation from nucleotide sequence
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x * 38660, sequence calculation, isozyme GSr2
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x * 38730, sequence calculation, isozyme GSr1
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x * 39200, sequence calculation, isozyme GS1a
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x * 39210, sequence calculation, isozyme GS1a
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x * 39240, sequence calculation, isozyme GS1c
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x * 39470, sequence calculation, isozyme GSe2
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x * 39480, sequence calculation, isozyme GSe1
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x * 46640, sequence calculation, isozyme GS2b, x * 41710, sequence calculation, mature peptide of isozyme GS2b
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x * 46690, sequence calculation, isozyme GS2a, x * 41760, sequence calculation, mature peptide of isozyme GS2a
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x * 46700, sequence calculation, isozyme GS2c, x * 41770, sequence calculation, mature peptide of isozyme GS2c
decamer
10 * 86000, cryo-electron microscopy
decamer
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10 * 60000, SDS-PAGE
decamer
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10 * 52000, SDS-PAGE
decamer
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x-ray crystallography
dimer
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2 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
dimer
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2 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
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dodecamer
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12 * 60000, SDS-PAGE
dodecamer
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composed of two hexameric rings
dodecamer
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type alpha12 dodecamer with oligomer and monomer having molecular weights of 630000 and 52000 Da, respectively
dodecamer
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composed of two hexameric rings
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dodecamer
isozyme GSI-alpha
dodecamer
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isozyme GSI-alpha
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dodecamer
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crystallization data
dodecamer
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12 * 63000, SDS-PAGE
dodecamer
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12 * 56000, SDS-PAGE
dodecamer
12 * 50500, about, sequence calculation
dodecamer
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12 * 58000, arranged in two superimpose hexagons, SDS-PAGE
dodecamer
crystal structure analysis, composed of two hexameric rings
dodecamer
Mtb-GlnA1 crystallizes in the space group P212121 with 24 monomers in the asymmetric unit to form a dodecamer. The 24 active sites of the dodecamer are found in long grooves between the subunits
dodecamer
MtGS is a dodecamer formed of two hexameric rings stacked on top of each other. Each active site includes contributions from two adjacent subunits within a ring
dodecamer
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Mtb-GlnA1 crystallizes in the space group P212121 with 24 monomers in the asymmetric unit to form a dodecamer. The 24 active sites of the dodecamer are found in long grooves between the subunits
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dodecamer
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MtGS is a dodecamer formed of two hexameric rings stacked on top of each other. Each active site includes contributions from two adjacent subunits within a ring
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dodecamer
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crystal structure analysis, composed of two hexameric rings
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dodecamer
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12 * 56000, SDS-PAGE
dodecamer
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12 * 58000, SDS-PAGE
dodecamer
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12 * 59000, SDS-PAGE
dodecamer
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12 * 50100, SDS-PAGE
dodecamer
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SDS-PAGE of 2-mercaptoethanol-treated enzyme
dodecamer
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12 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
dodecamer
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12 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
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dodecamer
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12 * 55000, SDS-PAGE
dodecamer
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12 * 55000, SDS-PAGE
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dodecamer
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12 * 55000, the enzyme exhibits different aggregation states with detectable oligomers of 1, 2, 3, 4, 6, 8, 10, and 12 subunits, SDS-PAGE
dodecamer
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12 * 55000, the enzyme exhibits different aggregation states with detectable oligomers of 1, 2, 3, 4, 6, 8, 10, and 12 subunits, SDS-PAGE
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dodecamer
12 * 52000, native mass by gel filtration, subunit mass calculated from amino acid sequence
dodecamer
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12 * 52000, enzyme form GSI, SDS-PAGE
dodecamer
12 * 50088, calculated from sequence
dodecamer
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12 * 50088, calculated from sequence
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dodecamer
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12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings
dodecamer
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12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings
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dodecamer
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12 * 52000, subunit mass by SDS-PAGE, native mass by gel filtration
dodecamer
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12 * 51000, SDS-PAGE
hexamer
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6 * 75000, isoform GS2, SDS-PAGE
hexamer
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6 * 70000, SDS-PAGE
hexamer
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6 * 70000, SDS-PAGE
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hexamer
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6 * 80000, enzyme form GSIII, SDS-PAGE
homooctamer
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8 * 44000, SDS-PAGE
homooctamer
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8 * 44000, SDS-PAGE
monomer
the enzyme is present in solution as monomer and as oligomer
monomer
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the enzyme is present in solution as monomer and as oligomer
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octamer
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8 * 43000, isoform GSII, SDS-PAGE
octamer
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8 * 47000, isoform GSI, SDS-PAGE
octamer
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8 * 51700, gel filtration
octamer
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8 * 44000, SDS-PAGE, composed of three different types of subunits with isoelectric points ranging from 7.0-7.2
octamer
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8 * 37400, subunit mass by SDS-PAGE, native mass by native PAGE
octamer
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8 * 43000, subunits by SDS-PAGE, native mass by gel filtration
octamer
8 * 42400, SDS-PAGE
octamer
8 * 43000, gel filtration
octamer
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8 * 48000, isoenzyme GScs, SDS-PAGE
octamer
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8 * 64000, isoenzyme GScl, SDS-PAGE
octamer
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8 * 48000, isoform GS2, SDS-PAGE
octamer
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8 * 38000, isoform GS1, SDS-PAGE
octamer
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x * 46500 + x * 49000, SDS-PAGE
octamer
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alpha, beta, 4 * 58000 + 4 * 65000, native mass by gel filtration, subunit mass by SDS-PAGE
octamer
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8 * 44000, enzyme form GS2, SDS-PAGE
oligomer
the enzyme is present in solution as monomer and as oligomer
oligomer
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the enzyme is present in solution as monomer and as oligomer
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trimer
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3 * 83000, recombinant isozyme GSIII-2, SDS-PAGE
trimer
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3 * 83000, recombinant isozyme GSIII-2, SDS-PAGE
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additional information
structure analysis, and comparison of mammalian, plant, and bacterial structures, overview
additional information
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structure analysis, and comparison of mammalian, plant, and bacterial structures, overview
additional information
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structure analysis, and comparison of mammalian, plant, and bacterial structures, overview