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tetramer
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4 * 42000, SDS-PAGE
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x * 51589, calculated
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x * 76400, calculated
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x * 45000, recombinant His-tagged enzyme, SDS-PAGE
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x * 45000, recombinant His-tagged enzyme, SDS-PAGE
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x * 54000, recombinant enzyme, SDS-PAGE
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x * 51800, recombinant His6-tagged enzyme, SDS-PAGE
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x * 45000, about, recombinant His6-tagged enzyme, SDS-PAGE
dimer
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2 * 42700, calculated
dimer
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enzyme crystal structure, the dimer interface is created by interactions between the catalytic and connecting regions of each subunit, a sulfate is bound at the expected site of the phosphate moiety of the sugar substrate, molecular replacement structure analysis and comparison, overview
dimer
2 * 41700, calculated and crystallization data
dimer
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enzyme crystal structure, the dimer interface is created by interactions between the catalytic and connecting regions of each subunit, a sulfate is bound at the expected site of the phosphate moiety of the sugar substrate, molecular replacement structure analysis and comparison, overview
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dimer
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2 * 41700, calculated and crystallization data
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dimer
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x * 42500, SDS-PAGE
dimer
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2 * 39000, SDS-PAGE
dimer
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crystallization data
homodimer
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additional information
enzyme CaDXR contains three conserved domain, namely NADPH (GSTGSIGT and LAAGSNV), substrate binding (LPADSEHSAI and NKGLEVIEAHY) and Cys-Ser-(Ala/Met/Val/Thr) cleavage-site domains. CaDXR is a basically alpha-helical protein which contains 21 alpha-helixes, 11 beta-sheets, and one hairpin structure
additional information
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enzyme CaDXR contains three conserved domain, namely NADPH (GSTGSIGT and LAAGSNV), substrate binding (LPADSEHSAI and NKGLEVIEAHY) and Cys-Ser-(Ala/Met/Val/Thr) cleavage-site domains. CaDXR is a basically alpha-helical protein which contains 21 alpha-helixes, 11 beta-sheets, and one hairpin structure
additional information
OsDXR has three highly conserved domains, including a proline-rich domain, two NADPH binding sites, and two substrate-binding sites
additional information
detailed three-dimensional modeling and analysis of structure-function relationship, comparative modeling through multiple alignment followed by intensive optimization, minimization, and validation, the three-dimensional structure shows monomeric subunit consisting of three domains: an N-terminal NADPH binding domain, a connective or linker domain, with most of the active site residues located in this domain, and a C-terminal domain
additional information
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detailed three-dimensional modeling and analysis of structure-function relationship, comparative modeling through multiple alignment followed by intensive optimization, minimization, and validation, the three-dimensional structure shows monomeric subunit consisting of three domains: an N-terminal NADPH binding domain, a connective or linker domain, with most of the active site residues located in this domain, and a C-terminal domain
additional information
a putative conserved cleavage site in the DXR motif is located at the N-terminus of PtDXR, and the NADPH-binding domains are involved in the transformation of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). Predicted tertiary structures of PtDXR, overview
additional information
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a putative conserved cleavage site in the DXR motif is located at the N-terminus of PtDXR, and the NADPH-binding domains are involved in the transformation of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). Predicted tertiary structures of PtDXR, overview