Crystallization (Comment) | Organism |
---|---|
mutant E201Q/N243D in complex with prodrug 2-fluoro-2'-deoxyadenosine and with 2-fluoroadenine. The overall fold of the mutant is nearly identical to the wild type enzyme. The residues Gln201 and Asp243 introduced by the mutation form hydrogen bond contacts with 2-fluoro-2'-deoxyadenosine that result in its binding and catalysis. Comparison of complexes suggest that the side chains of Gln201 and Asp243 as well as the purine base rotate during catalysis possibly facilitating cleavage of the glycosidic bond | Homo sapiens |
Protein Variants | Comment | Organism |
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E201Q/N243D | crystallization data | Homo sapiens |
Organism | UniProt | Comment | Textmining |
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Homo sapiens | P00491 | - |
- |