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x * 28000, SDS-PAGE
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x * 41000, recombinant His-tagged enzyme, SDS-PAGE, x * 41400, about, full-length enzyme, sequence calculation, x * 41260, enzyme without signal peptide, sequence calculation
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x * 41400, about, isozyme BmCDA7 , sequence calculation
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x * 41500, about, isozyme BmCDA8 , sequence calculation
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x * 41700, about, isozyme BmCDA6, sequence calculation
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x * 61000, about, isozyme B, sequence calculation
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x * 62000, about, isozyme A, sequence calculation
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S1-CDA: 24700, S1-CDAH: 25700, S12-CDAH: 26800, original CDA: 24300, SDS-PAGE
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x * 25756, electrospray ionization MS
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x * 25200, recombinant His6-tagged enzyme, SDS-PAGE
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x * 25200, recombinant His6-tagged enzyme, SDS-PAGE
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x * 33000, isozyme 1, SDS-PAGE, x * 55000, isozyme 2, SDS-PAGE
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x * 29668, CDA2, amino acid sequence calculation
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x * 32504, CDA1, amino acid sequence calculation
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x * 34264, CDA3, amino acid sequence calculation
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x * 53000, SDS-PAGE
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x * 48700, about, sequence calculation, x * 26800, recombinant Strep-tagged catalytic domain, SDS-PAGE
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x * 48700, about, sequence calculation, x * 26800, recombinant Strep-tagged catalytic domain, SDS-PAGE
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x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE
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x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE
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x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE
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x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE
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x * 40000, about, sequence calculation, x * 35500, recombinant enzyme, SDS-PAGE
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x * 28500, recombinant His-tagged enzyme, SDS-PAGE
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 66000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 129000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 43000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 45000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 56000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 60000, calculated from sequence
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A7U8C9, A7U8D0, A7U8D1, A8W488, A8W489, A8W490, A8W491, A8W492, A8W493, A8W494, A8W495 x * 62000, calculated from sequence
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x * 43000, recombinant enzyme, SDS-PAGE
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5 isozymes of 48100, 30700, 25200, 15200 and 12700 Da respectively, substrate SDS-PAGE i.e. SDS-PAGE in presence of substrate
monomer
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1 * 75000, SDS-PAGE
monomer
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1 * 150000, amino acid and carbohydrate analysis in combination with data from SDS-PAGE and gel filtration
monomer
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1 * 31500-33000, SDS-PAGE
monomer
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1 * 52000, SDS-PAGE
monomer
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1 * 52000, SDS-PAGE
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monomer
1 * 100000, gel filtration
monomer
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1 * 43000, SDS-PAGE
monomer
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1 * 55000, SDS-PAGE
additional information
A0A1U8QU02
three-dimensional and secondary structure analysis
additional information
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three-dimensional and secondary structure analysis
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additional information
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three-dimensional and secondary structure analysis
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additional information
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three-dimensional and secondary structure analysis
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additional information
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three-dimensional and secondary structure analysis
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additional information
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three-dimensional and secondary structure analysis
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additional information
comparison of enzyme amino acid sequences of strain UPS9 with those of strain ATCC 56676, overview
additional information
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comparison of enzyme amino acid sequences of strain UPS9 with those of strain ATCC 56676, overview
additional information
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comparison of enzyme amino acid sequences of strain UPS9 with those of strain ATCC 56676, overview
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additional information
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peptide mass fingerprinting of both isozymes, MALDI-TOF mass spectrometry, the enzyme has a large C-terminal extracellular domain and a transmembrane domain
additional information
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CDA1 amino acid sequence and structure modelling
additional information
the enzyme contains a signal peptide, a chitin-binding domain, a low-density lipoprotein receptor class A domain, and a polysaccharide deacetylase-like catalytic domain
additional information
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the enzyme contains a signal peptide, a chitin-binding domain, a low-density lipoprotein receptor class A domain, and a polysaccharide deacetylase-like catalytic domain
additional information
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the enzyme contains a signal peptide, a chitin-binding domain, and a chitin deacetylase catalytic domain
additional information
the enzyme contains a signal peptide, a chitin-binding domain, and a chitin deacetylase catalytic domain
additional information
the enzyme contains four structural domains: a signal peptide, a chitin-binding peritrophin-A domain, a low-density lipoprotein receptor class A (LDLa) domain, and a catalytic domain
additional information
the enzyme contains four structural domains: a signal peptide, a chitin-binding peritrophin-A domain, a low-density lipoprotein receptor class A (LDLa) domain, and a catalytic domain
additional information
the enzyme contains four structural domains: a signal peptide, a chitin-binding peritrophin-A domain, a low-density lipoprotein receptor class A (LDLa) domain, and a catalytic domain
additional information
domain architecture of the chitin deacetylase PesCDA from Pestalotiopsis sp.. The enzyme contains an N-terminal putative signal peptide (SP), a polysaccharide deacetylase domain (PDD), and a C-terminal carbohydrate binding module representing motif family 18 (CBM18)
additional information
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domain architecture of the chitin deacetylase PesCDA from Pestalotiopsis sp.. The enzyme contains an N-terminal putative signal peptide (SP), a polysaccharide deacetylase domain (PDD), and a C-terminal carbohydrate binding module representing motif family 18 (CBM18)
additional information
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the enzyme protein is composed of the CE4 domain flanked by two CBM18 domains
additional information
the secondary structure consists of a conserved (alpha/beta)8 folded barrel structure and six loops. Structure comparisons, overview
additional information
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the secondary structure consists of a conserved (alpha/beta)8 folded barrel structure and six loops. Structure comparisons, overview
additional information
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the secondary structure consists of a conserved (alpha/beta)8 folded barrel structure and six loops. Structure comparisons, overview
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