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 | Geranylgeranyl transferase type-1 subunit beta |
Enzyme Information
| 2.5.1.59 |
Protein geranylgeranyltransferase type I.
based on mapping to UniProt P53610
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl- protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 atom of the geranylgeranyl 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 leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. -!- The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding.
|
UniProtKB Entries (1)
| P53610 |
PGTB1_RAT
Rattus norvegicus
Geranylgeranyl transferase type-1 subunit beta
|
PDB Structure
| PDB | 1S64 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Spodoptera |
| Primary Citation |
Crystallographic Analysis Reveals that Anticancer Clinical Candidate L-778,123 Inhibits Protein Farnesyltransferase and Geranylgeranyltransferase-I by Different Binding Modes.
Biochemistry
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