1JCQ
CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750
Summary for 1JCQ
Entry DOI | 10.2210/pdb1jcq/pdb |
Related | 1D8D 1FT1 1JCR 1JCS |
Related PRD ID | PRD_900003 |
Descriptor | PROTEIN FARNESYLTRANSFERASE, ALPHA SUBUNIT, PROTEIN FARNESYLTRANSFERASE, BETA SUBUNIT, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ... (8 entities in total) |
Functional Keywords | ftase, pft, pftase, ft, fpt, farnesyltransferase, farnesyl transferase, farnesyl protein transferase, caax, ras, cancer, tumor regression, l-739, 750, peptidomimetic, inhibitor, transferase |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 95055.03 |
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 citation | Long, 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: 11687658DOI: 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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