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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1crystal structure of the enzyme in complex with substrate analoge delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine and Fe(II) at 1.40 A resolution reveals that the compound binds in the active site such that the sulfur atom of the methionine thioether binds to iron in the oxygen binding site at a distance of 2.57 A. The sulfur of the cysteinyl thiolate sits 2.36 A from the metal
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1crystal structure of the enzyme reveals that the active site of IPNS is buried in a characteristic jelly-roll motif that has been found in other oxygenases
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1crystal structure, molecular modeling of the active site structure and the Fe2+-binding motif
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1enzyme complexed with manganese instead of iron in the active site, more stable
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1in complex with substrat analogue delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine and Fe(II). Structure reveals an additional water molecule bound to the active site metal, held by hydrogen-bonding to the ether oxygen atom of the substrate analogue
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1in complex with substrate analogue delta-(L-alpha-aminoadipoyl)-(3R)-methyl-L-cysteine D-alpha hydroxyvaleryl ester, crystallization with anaerobic conditions and exposure of crystals to oxygen giving a hydroxymethyl/ene product. Discussion of steric and electronic effects around the valinyl isopropyl side chain of the enzyme’s active side
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1in complex with substrate homologues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine. The complex with Fe(II) and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine shows diffuse electron density for several regions of the substrate, revealing considerable conformational freedom within the active site. The substrate is more clearly resolved in the complex delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine by virtue of thioether coordination to iron. delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine occupies two distinct conformations, both distorted relative to the natural substrate (L-alha-aminoadipoyl)-L-cysteinyl-D-valine, in order to accommodate the extra methylene group in the second residue
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1in complex with tripeptyl analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-beta-methyl-D-cyclopropylglycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-cyclopropylglycine, crystallization in presence of Fe-(II) under anaerobic conditions
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1in complex with truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine in presence of Fe(II) and presence and absence of nitric oxide. C-terminal carboxylate of substrate is oriented toward the active site iron atom
Display the word mapDisplay the reaction diagram Show all sequences 1.21.3.1structure analysis
Results 1 - 10 of 12 > >>