CATH Domain 2g62A02

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.20	Up-down Bundle
	1.20.120	Four Helix Bundle (Hemerythrin (Met), subunit A)
	1.20.120.1150	Phosphotyrosyl phosphate activator, C-terminal lid domain

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	2G62
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions. Magnusdottir, A., Stenmark, P., Flodin, S., Nyman, T., Hammarstrom, M., Ehn, M., Bakali H, M.A., Berglund, H., Nordlund, P. J.Biol.Chem.