Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.59 extracted from

  • Reid, T.S.; Long, S.B.; Beese, L.S.
    Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes (2004), Biochemistry, 43, 9000-9008.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
low-affinity ternary complex of L-778,123 bound in GGTase-I peptide-binding site and geranylgeranyl diphosphate bound in the lipid-binding site and complex of GGTase-I with L-778,123 and a sulfate anion Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
L-778,123
-
Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Synonyms

Synonyms Comment Organism
GGTase-I
-
Rattus norvegicus