Crystallization (Comment) | Organism |
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crystal 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 | Aspergillus nidulans |
Inhibitors | Comment | Organism | Structure |
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delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine | substrate analogue, which incorporates a thioether in place of the valinyl sidechain. Crystal structure of the enzyme in complex with the compound 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 | Aspergillus nidulans |
Organism | UniProt | Comment | Textmining |
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Aspergillus nidulans | P05326 | - |
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Aspergillus nidulans ATCC 38163 | P05326 | - |
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