Title : The interactions of metal cations and oxyanions with protein tyrosine phosphatase 1B.

Pub. Date : 2017 Aug

PMID : 28540523






1 Functional Relationships(s)
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1 In contrast to zinc, which binds to the phosphocysteine intermediate in the closed conformation of protein tyrosine phosphatase 1B when the catalytic aspartate has moved into the active site, other divalent cations such as cadmium and copper may also bind to the enzyme in the open conformation. Aspartic Acid protein tyrosine phosphatase non-receptor type 1 Homo sapiens