Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 65000, SDS-PAGE
?
-
x * 70000, calculated from amino acid sequence
?
-
x * 70000, calculated from amino acid sequence
-
?
-
x * 60700, wild-type, calculated, x * 61000, wild-type, SDS-PAGE, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 68202, sequence calculation, x * 65237, mass spectrometry
?
x * 67000, recombinant enzyme, SDS-PAGE
?
-
x * 67000, recombinant enzyme, SDS-PAGE
-
?
WP_028494267
x * 112000, SDS-PAGE
?
-
x * 110000, calculation from nucleotide sequence
?
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
?
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 63300, about, sequence calculation
dimer
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
dimer
-
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
-
dimer
DrTS consists of a catalytic (beta/alpha)8 barrel, subdomain B, a C-terminal beta-domain and two TS-unique subdomains, S7 and S8. The C-terminal domain and domain S8 contribute the majority of the dimeric interface, analytical ulatracentrifugation. Enzyme structure comparisons, detailed overview
dimer
2 * 68000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
-
homodimer
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
homodimer
-
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
-
homohexamer
-
6 * 65000, SDS-PAGE
homohexamer
-
6 * 68000, gel filtration
homohexamer
-
6 * 65000, SDS-PAGE
homohexamer
-
6 * 68000, gel filtration
tetramer
-
tetramer
-
4 * 67000, SDS-PAGE
tetramer
-
4 * 67000, SDS-PAGE
-
additional information
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
additional information
-
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
additional information
-
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
-
additional information
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
-
additional information
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
additional information
-
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
additional information
-
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
-
additional information
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
additional information
-
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
additional information
-
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
-
additional information
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
-