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1JCQ

CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750

Summary for 1JCQ
Entry DOI10.2210/pdb1jcq/pdb
Related1D8D 1FT1 1JCR 1JCS
Related PRD IDPRD_900003
DescriptorPROTEIN FARNESYLTRANSFERASE, ALPHA SUBUNIT, PROTEIN FARNESYLTRANSFERASE, BETA SUBUNIT, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ... (8 entities in total)
Functional Keywordsftase, pft, pftase, ft, fpt, farnesyltransferase, farnesyl transferase, farnesyl protein transferase, caax, ras, cancer, tumor regression, l-739, 750, peptidomimetic, inhibitor, transferase
Biological sourceHomo sapiens (human)
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Total number of polymer chains2
Total formula weight95055.03
Authors
Long, S.B.,Casey, P.J.,Beese, L.S. (deposition date: 2001-06-11, release date: 2001-11-02, Last modification date: 2023-08-16)
Primary citationLong, S.B.,Hancock, P.J.,Kral, A.M.,Hellinga, H.W.,Beese, L.S.
The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Proc.Natl.Acad.Sci.USA, 98:12948-12953, 2001
Cited by
PubMed: 11687658
DOI: 10.1073/pnas.241407898
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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