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Structure paper

TitleResistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Journal, issue, pagesMol. Biochem. Parasitol., Vol. 152, Page 66-71, Year 2007
Publish dateSep 19, 2006 (structure data deposition date)
AuthorsEastman, R.T. / White, J. / Hucke, O. / Yokoyama, K. / Verlinde, C.L. / Hast, M.A. / Beese, L.S. / Gelb, M.H. / Rathod, P.K. / Van Voorhis, W.C.
External linksMol. Biochem. Parasitol. / PubMed:17208314
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-2iej:
Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-ZN:
Unknown entry

ChemComp-S48:
METHYL N-{(3S)-1-[(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-6-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-3-YL}-N-[(1-METHYL-1H-IMIDAZOL-4-YL)SULFONYL]GLYCINATE

ChemComp-FII:
[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / FTASE / FARNESYLTRANSFERASE / FARNESYL TRANSFERASE / CAAX / RAS / CANCER / TUMOR REGRESSION / STN-48 / PROTEIN PRENYLATION / LIPID MODIFICATION / PLASMODIUM / FALCIPARUM / MALARIA

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