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 P49356
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)

P49356
FNTB_HUMAN
Homo sapiens
Protein farnesyltransferase subunit beta

PDB Structure

PDB 1LD7
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency.
Bell, I.M., Gallicchio, S.N., Abrams, M., Beese, L.S., Beshore, D.C., Bhimnathwala, H., Bogusky, M.J., Buser, C.A., Culberson, J.C., Davide, J., Ellis-Hutchings, M., Fernandes, C., Gibbs, J.B., Graham, S.L., Hamilton, K.A., Hartman, G.D., Heimbrook, D.C., Homnick, C.F., Huber, H.E., Huff, J.R., Kassahun, K., Koblan, K.S., Kohl, N.E., Lobell, R.B., Lynch Jr., J.J., Robinson, R., Rodrigues, A.D., Taylor, J.S., Walsh, E.S., Williams, T.M., Zartman, C.B.
J.Med.Chem.