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TitleCrystallographic Analysis Reveals that Anticancer Clinical Candidate L-778,123 Inhibits Protein Farnesyltransferase and Geranylgeranyltransferase-I by Different Binding Modes.
Journal, issue, pagesBiochemistry, Vol. 43, Page 9000-9008, Year 2004
Publish dateJan 22, 2004 (structure data deposition date)
AuthorsReid, T.S. / Long, S.B. / Beese, L.S.
External linksBiochemistry / PubMed:15248757
MethodsX-ray diffraction
Resolution1.9 - 2.55 Å
Structure data

PDB-1s63:
Human protein farnesyltransferase complexed with L-778,123 and FPP
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1s64:
Rat protein geranylgeranyltransferase type-I complexed with L-778,123 and a sulfate anion
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-FPP:
FARNESYL DIPHOSPHATE

ChemComp-778:
4-[(5-{[4-(3-CHLOROPHENYL)-3-OXOPIPERAZIN-1-YL]METHYL}-1H-IMIDAZOL-1-YL)METHYL]BENZONITRILE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / FARNESYLTRANSFERASE / FTASE / GERANYLGERANYLTRANSFERASE / CANCER / CAAX / FTI / INHIBITOR / RAS / LIPID MODIFICATION / PROTEIN PRENYLATION / L-778 / 123 / protein geranylgeranyltransferase type-I / drug

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