CATH Classification

Domain Context

CATH Clusters

Functional Family Protein farnesyltransferase subunit beta

Enzyme Information
Protein farnesyltransferase.
based on mapping to UniProt Q02293
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
-!- This enzyme, along with EC and EC, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.

UniProtKB Entries (1)

Rattus norvegicus
Protein farnesyltransferase subunit beta

PDB Structure

External Links
Organism Spodoptera
Primary Citation
The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Long, S.B., Hancock, P.J., Kral, A.M., Hellinga, H.W., Beese, L.S.