Crystallization (Comment) | Organism |
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in ligand-free form and in complexes with inhibitor oxonate, physiological substrates and products of the first and second half-reactions. Ligands bind to the same active site of enzyme, consistent with one-site ping-pong Bi-Bi mechanism. The binding of ligands does not cause any significant structural changes, and both reduced and oxidized FMN cofactors are in planar conformation. Resiude C130 is well located for abstracting a proton from dihydroorotate C5 and transferring it to outside water molecules. The bound fumarate is in a twisted conformation, which induces partial charge separation. The thermodynamically favorable reduction of fumarate with reduced FMN seems to proceed in the way that its C2 accepts a proton from C130 and C3 a hydride or a hydride equivalent from reduced FMN N5 | Trypanosoma cruzi |
Inhibitors | Comment | Organism | Structure |
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oxonate | crystallization data | Trypanosoma cruzi |
Organism | UniProt | Comment | Textmining |
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Trypanosoma cruzi | Q4D3W2 | - |
- |