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x * 37000, SDS-PAGE
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x * 37000, about, recombinant enzyme, SDS-PAGE
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x * 37000, about, recombinant enzyme, SDS-PAGE
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dimer
2 * 36000, SDS-PAGE
dimer
enzyme AfASADH displays a crystallographic dimer
dimer
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enzyme AfASADH displays a crystallographic dimer
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dimer
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2 * 38000, SDS-PAGE
dimer
crystal structure, subdomain structure of subunits, open and closed enzyme forms
dimer
the central part of the dimerization domain is a sixstranded beta-sheet consisting of two pairs of parallel beta-strands flanking two central antiparallel strands. The sheets are oriented parallel to the sheet of the second subunit so that many interactions can occur between the side chains of nearby residues. Hydrogen bonds are formed between Thr257 and Asn157, between the two Ser159 residues, and between Tyr161 and the carbonyl O atom of Thr160. A buried hydrophobic patch is also formed by Ile260, Phe341 and Ala273. There are two highly charged regions at opposite ends of the beta-sheet. The subunit assembly aligns these highly charged regions in the dimer. These patches are formed by residues 327-336 of a loop in the beta-sheet and residues 214-236 of the arm. A series of salt bridges are formed in this region by Arg327, Glu238, Lys329, Asp258 and His339
dimer
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the central part of the dimerization domain is a sixstranded beta-sheet consisting of two pairs of parallel beta-strands flanking two central antiparallel strands. The sheets are oriented parallel to the sheet of the second subunit so that many interactions can occur between the side chains of nearby residues. Hydrogen bonds are formed between Thr257 and Asn157, between the two Ser159 residues, and between Tyr161 and the carbonyl O atom of Thr160. A buried hydrophobic patch is also formed by Ile260, Phe341 and Ala273. There are two highly charged regions at opposite ends of the beta-sheet. The subunit assembly aligns these highly charged regions in the dimer. These patches are formed by residues 327-336 of a loop in the beta-sheet and residues 214-236 of the arm. A series of salt bridges are formed in this region by Arg327, Glu238, Lys329, Asp258 and His339
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dimer
2 * 37000, about, recombinant His-tagged enzyme, SDS-PAGE
dimer
dimerization domain structure, overview
dimer
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dimerization domain structure, overview
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dimer
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2 * 44000, SDS-PAGE
dimer
crystal structure, communication mechanism between the active sites of the subunits, overview
homodimer
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homodimer
x-ray crystallography
homodimer
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crystallization
homodimer
recombinant enzyme
homodimer
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recombinant enzyme
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homodimer
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2 * 39000, SDS-PAGE
homodimer
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crystallization
homotetramer
dimer-of-dimers
homotetramer
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dimer-of-dimers
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homotetramer
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dimer-of-dimers
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tetramer
dimer of dimers, 4 * 40000, about, recombinant His-tagged enzyme, SDS-PAGE
tetramer
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dimer of dimers, 4 * 40000, about, recombinant His-tagged enzyme, SDS-PAGE
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tetramer
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4 * 41000, SDS-PAGE
tetramer
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4 * 39530, nucleotide sequence analysis of the HOM2 region
additional information
enzyme secondary structure, crystal structure analysis, detailed overview
additional information
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enzyme secondary structure, crystal structure analysis, detailed overview
additional information
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enzyme secondary structure, crystal structure analysis, detailed overview
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additional information
enzyme secondary structure, crystal structure analysis and comparisons, the C-terminal domain consists of six beta-strands, six alpha-helices and a single 310-helix that represent the catalytic site and the dimerization interface, detailed overview
additional information
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enzyme secondary structure, crystal structure analysis and comparisons, the C-terminal domain consists of six beta-strands, six alpha-helices and a single 310-helix that represent the catalytic site and the dimerization interface, detailed overview
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additional information
the asymmetric unit contains three subunits: one complete dimer and a monomer which comes from a dimer lying along the crystallographic 2fold axis
additional information
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the asymmetric unit contains three subunits: one complete dimer and a monomer which comes from a dimer lying along the crystallographic 2fold axis
additional information
secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
additional information
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secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
additional information
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secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
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