Crystallization (Comment) | Organism |
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structures of wild-type in complex with H2O2, and the catalytically inactive Y379F mutant in complex with palmitic acid. PA binds within the active site cleft of alpha-DOX such that the carboxylate forms ionic interactions with residues His311 and Arg559. Thr316 aids in the positioning of carbon-2 for hydrogen abstraction. The binding of H2O2 at the distal face of the heme displaces residues His157, Asp158, and Trp159 about 2.5 A from their positions in the wild type structure | Oryza sativa |
Organism | UniProt | Comment | Textmining |
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Oryza sativa | Q9M5J1 | - |
- |