CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.50 | Alpha/alpha barrel |
|
1.50.10 | Glycosyltransferase |
|
1.50.10.20 |
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)
| Q04631 |
FNTA_RAT
Rattus norvegicus
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
|
PDB Structure
| PDB | 4GTR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Development of Selective, Potent RabGGTase Inhibitors
J.Med.Chem.
|
