CATH Classification

Domain Context

CATH Clusters

Superfamily Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain
Functional Family

Enzyme Information

5.2.1.8
Peptidylprolyl isomerase.
based on mapping to UniProt Q5ZXE0
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)

Q5ZXE0
MIP_LEGPH
Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Outer membrane protein MIP

PDB Structure

PDB 1FD9
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of Mip, a prolylisomerase from Legionella pneumophila
Riboldi-Tunnicliffe, A., Konig, B., Jessen, S., Weiss, M.S., Rahfeld, J., Hacker, J., Fischer, G., Hilgenfeld, R.
Nat.Struct.Biol.