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MineSummary [2iej]

Summary Structural Experimental Function Sequence Neighbor Download Link

<Asymmetric unit>
= <Biological unit>

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PDB ID2iej  sequence information (FASTA format)   
DescriptorProtein farnesyltransferase/geranylgeranyltransferase type I alpha subunit (E.C.2.5.1.58, 2.5.1.59), Protein farnesyltransferase subunit beta (E.C.2.5.1.58)
TitleHuman Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution
Functional KeywordsFTASE, FARNESYLTRANSFERASE, FARNESYL TRANSFERASE, CAAX, RAS, CANCER, TUMOR REGRESSION, STN-48, PROTEIN PRENYLATION, LIPID MODIFICATION, PLASMODIUM, FALCIPARUM, MALARIA
Biological sourceHomo sapiens (human)
Organ source [UNP - P49354] Retina
[UNP - P49354] Placenta
[UNP - P49354] Colon, and Lung
Total number of polymer chains2
Total molecular weight95285 (the details in Structural Details Page)
AuthorsHast, M.A. , Beese, L.S. (deposition date : 2006-09-19, release date : 2007-01-23)
Primary citationEastman, 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.
Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Mol.Biochem.Parasitol., 152:66 - 71, 2007.(PubMed : 17208314)  (DOI: 10.1016/j.molbiopara.2006.11.012)
Experimental methodX-RAY DIFFRACTION ( 1.800[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P49354, P49356 ) , eF-site , KEGG ( EC 2.5.1.58, 2.5.1.59 ) , PISA