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The catalytic mechanism of the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2)

Fig 3

(a) NAD+ and Pi binding site from the X-ray structure (6KG2.pdb). Each monomer is labeled as subunit A (green) and B (cyan), respectively. Asp168, Asp216 and Asp225 from subunit B are colored as cyan for C atoms and shown as sticks. The minimum distance between Asp168 and Asp225 is 7.9Å. (b) The MgA binding pocket. (c) The MgB binding pocket.

Fig 3

doi: https://doi.org/10.1371/journal.pcbi.1010140.g003