CATH Classification

Domain Context

CATH Clusters

Superfamily 1.20.120.1150
Functional Family Serine/threonine-protein phosphatase 2A activator

Enzyme Information

5.2.1.8
Peptidylprolyl isomerase.
based on mapping to UniProt Q15257
Peptidylproline (omega=180) = peptidylproline (omega=0).
-!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.

UniProtKB Entries (1)

Q15257
PTPA_HUMAN
Homo sapiens
Serine/threonine-protein phosphatase 2A activator

PDB Structure

PDB 4NY3
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A.
Low, C., Quistgaard, E.M., Kovermann, M., Anandapadamanaban, M., Balbach, J., Nordlund, P.
Biol.Chem.
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