CATH Classification

Domain Context

CATH Clusters

Superfamily 1.50.10.20
Functional Family Protein farnesyltransferase subunit beta

Enzyme Information

2.5.1.58
Protein farnesyltransferase.
based on mapping to UniProt Q02293
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, 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 2.5.1.59. -!- 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)

Q02293
FNTB_RAT
Rattus norvegicus
Protein farnesyltransferase subunit beta

PDB Structure

PDB 1X81
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Design, synthesis, and activity of 4-quinolone and pyridone compounds as nonthiol-containing farnesyltransferase inhibitors.
Li, Q., Claiborne, A., Li, T., Hasvold, L., Stoll, V.S., Muchmore, S., Jakob, C.G., Gu, W., Cohen, J., Hutchins, C., Frost, D., Rosenberg, S.H., Sham, H.L.
Bioorg.Med.Chem.Lett.