CATH Classification

Domain Context

CATH Clusters

Superfamily 2.40.10.330
Functional Family Peptidyl-prolyl cis-trans isomerase

Enzyme Information

5.2.1.8
Peptidylprolyl isomerase.
based on mapping to UniProt P0A9K9
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)

P0A9K9
SLYD_ECOLI
Escherichia coli K-12
FKBP-type peptidyl-prolyl cis-trans isomerase SlyD

PDB Structure

PDB 2KFW
External Links
Method SOLUTION NMR
Organism
Primary Citation
The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity.
Martino, L., He, Y., Hands-Taylor, K.L., Valentine, E.R., Kelly, G., Giancola, C., Conte, M.R.
Febs J.