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dimer
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2 * 73000, SDS-PAGE
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x * 38000, SDS-PAGE
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x * 38000, SDS-PAGE
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x * 39200, calculated from amino acid sequence
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x * 34300, calculated from amino acid sequence
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x * 34000, SDS-PAGE
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x * 34300, calculated from amino acid sequence
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x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
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x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
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x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
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x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
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x * 60000, SDS-PAGE, recombinant enzyme
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x * 60000, SDS-PAGE
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x * 56000, SDS-PAGE, x * 43847, calculated
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x * 56000, SDS-PAGE, x * 46644, calculated
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x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
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x * 56000, SDS-PAGE, x * 43847, calculated
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x * 56000, SDS-PAGE, x * 46644, calculated
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x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
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x * 37700, calculated
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x * 53000, SDS-PAGE
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x * 37700, calculated
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x * 45000, SDS-PAGE
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x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
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x * 45000, SDS-PAGE, x * 41000, calculated
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x * 38000, native purified enzyme, SDS-PAGE
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x * 54000, recombinant protein, SDS-PAGE
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x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
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x * 41000, recombinant enzyme, SDS-PAGE
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x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
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x * 41000, recombinant enzyme, SDS-PAGE
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x * 39600, SDS-PAGE
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x * 40000, SDS-PAGE
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x * 44000, SDS-PAGE, x * 43767, calculated
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x * 44000, SDS-PAGE, x * 43767, calculated
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x * 70000, SDS-PAGE, recombinant protein including His-tag
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x * 43000, ManB, SDS-PAGE
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x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
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x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
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x * 43000, SDS-PAGE
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x * 32000, calculated and SDS-PAGE
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x * 31000, SDS-PAGE
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x * 32000, calculated and SDS-PAGE
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x * 145294, calculated
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x * 145294, calculated
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x * 53600, calculated
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x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
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x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
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x * 43000, recombinant enzyme, SDS-PAGE
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x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
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x * 42400, deduced from gene sequence, mature protein
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x * 60000, SDS-PAGE of recombinant protein, x * 50605, calculated
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x * 44000, SDS-PAGE
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x * 65000-70000, His6-tagged enzyme, SDS-PAGE
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x * 65000-70000, His6-tagged enzyme, SDS-PAGE
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x * 33000, SDS-PAGE and calculated
monomer
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1 * 66000, SDS-PAGE
monomer
1 * 40000, SDS-PAGE, 1 * 40457, calculated
monomer
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1 * 40000, SDS-PAGE, 1 * 40457, calculated
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monomer
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1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
monomer
1 * 50000, SDS-PAGE
monomer
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1 * 50000, SDS-PAGE
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monomer
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1 * 38000, SDS-PAGE
monomer
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1 * 38000, SDS-PAGE
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monomer
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
monomer
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1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
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monomer
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1 * 36250, SDS-PAGE
monomer
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1 * 36450, calculated from amino acid sequence
monomer
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1 * 36250, SDS-PAGE
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monomer
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1 * 36450, calculated from amino acid sequence
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additional information
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the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
additional information
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the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
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additional information
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the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
additional information
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the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
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additional information
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Trp360 is critical in substrate binding at -1 subsite, Tyr285 works as nucleophile catalyst, Trp217 and Trp162 are important for the activity against mannooligosaccharides but less important for activity against polysaccharides
additional information
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
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the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
the enzyme adopts the (beta/alpha)8-barrel fold
additional information
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the enzyme adopts the (beta/alpha)8-barrel fold
additional information
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the enzyme adopts the (beta/alpha)8-barrel fold
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additional information
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
additional information
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
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the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
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the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
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the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
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additional information
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the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
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