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docking models for inhibitor (3-[hydroxy(5-oxohexanoyl)amino]propyl)phosphonic acid based on crystal structure in complex with fosmidomycin. Formation of a hydrogen bond between an appropriately placed carbonyl group in the acyl residue and the main-chain NH of M214 located in the flexible catalytic loop of the enzyme
in complex with inhibitor [(1-isoquinolinylamino)methylene]-1,1-bisphosphonate and in complex with inhibitor [[(5-chloro-2-pyridinyl)amino]methylene]-1,1-bisphosphonate
in complex with Mg2+, NADPH, and inhibitor fosmidomycin. Protein exhibits a well-ordered conformation upon substrate binding. No electron density is observed for the nicotinamide-ribose portion of NADPH and the position of D149 anchoring Mg2+ is shifted by NADPH in the active site
selenomethionine labelled enzyme in ternary complex with the antimalarial compound fosmidomycin and NADPH
homology modeling based on the Escherichia coli homolog
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homology modeling of structure
MtDXR in complex with fosmidomycin alone or additionally with inhibitor 3-(N-hydroxyacetamido)-1-(3,4-dichlorophenyl)propylphosphonic acid or inhibitor 3-(N-hydroxyformamido)-1-(3,4-dichlorophenyl)propylphosphonic acid and NADPH, from 25% w/v PEG 3350, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.7-5.9, a cryosolution consists of the screening solution and 25% glycerol, 75 mM NaCl including DMSO, dithiothreitol, cofactors Mn2+ and NADPH, and ligands, i.e. compounds 3-(N-hydroxyformamido)-1-(3,4-dichlorophenyl)propylphosphonic acid and 3-(N-hydroxyacetamido)-1-(3,4-dichlorophenyl)propylphosphonic acid, X-ray diffraction structure determination and analysis
purified recombinant His-tagged enzyme with inhibitor fosmidomycin, microbatch method, sitting drops mixed from 0.001 ml of protein solution, containing 5 mg/ml protein in 150 mM NaCl and 20 mM TrisHCl pH 7.5, and 0.001 ml of crystallization buffer, containing 40% ethylene glycol, 2 mM MgSO4, 20 mM DTT, 0.2 mM EDTA and 100 mM acetate pH 5.0, streak-seeded immediately with a horse hair, 4 weeks, stabilization prior to flash-cooling in reservoir solution complemented with additional 10% ethylene glycol and 1 mM fosmidomycin, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
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wild-type and mutant D151N/E222Q in various complexes with Mn2+, NADPH, and inhibotr fosmidomycin. Asymmetric unit corresponds to biological homodimer. Crystal contacts stabilize an open active site in the B molecule, the A molecule displays closed conformation
generation of homology model and ligand docking studies
hanging-drop vapour-diffusion method in the presence of NADPH, data to 1.85 A resolution. Space group C2
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in complex with NADPH and Mg2+, and in complex with fosmidomycin, NADPH and Mg2+, both to 2.0 A resolution
purified recombinant enzyme in apoform, or in complex with inhibitors fosmidomycin or FR900098 and Mn2+, or in complex with arginine, or in phosphate-free condition, hanging and sitting drop vapor diffusion methods, mixing of 12 mg/ml protein in 10 mM Tris-HCl, pH 7.4, and 150 mM NaCl, at 25°C, with reservoir solution of different compositions, crystallization conditions, overview, X-ray diffraction structure determination and analysis, molecular replacement using the Escherichia coli Dxr enzyme structure (PDB ID 1Q0L) as a starting model, modeling
apo-form and binary complex with NADPH
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