B8CC74C5E1FA93951820CD25F505C621C4E6EF29E3653E3B5F01DBEAC944D0DB8E7BD1B29BA95394E58D936F2A2F93FE

Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation (By similarity). Forms oligomers. Has been reported as a homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin.

Source:http://purl.uniprot.org/SHA-384/B8CC74C5E1FA93951820CD25F505C621C4E6EF29E3653E3B5F01DBEAC944D0DB8E7BD1B29BA95394E58D936F2A2F93FE

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Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation (By similarity). Forms oligomers. Has been reported as a homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin.