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1SA4

human protein farnesyltransferase complexed with FPP and R115777

Summary for 1SA4
Entry DOI10.2210/pdb1sa4/pdb
Related1D8D 1FT1 1JCQ 1JCR 1LD8 1O5M 1SA5
Related PRD IDPRD_900003
DescriptorProtein farnesyltransferase/geranylgeranyltransferase type I alpha subunit, Protein farnesyltransferase beta subunit, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ... (7 entities in total)
Functional Keywordsftase, farnesyltransferase, farnesyl transferase, caax, ras, cancer, tumor regression, r115777, tipifarnib, zarnestra, fti, clinical candidate, inhibitor, protein prenylation, lipid modification, transferase
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight94966.67
Authors
Reid, T.S.,Beese, L.S. (deposition date: 2004-02-06, release date: 2004-06-08, Last modification date: 2023-08-23)
Primary citationReid, T.S.,Beese, L.S.
Crystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and BMS-214662 Complexed with Protein Farnesyltransferase Suggest a Mechanism of FTI Selectivity.
Biochemistry, 43:6877-6884, 2004
Cited by
PubMed: 15170324
DOI: 10.1021/bi049723b
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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