1TN8
Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution
Summary for 1TN8
Entry DOI | 10.2210/pdb1tn8/pdb |
Related | 1D8D 1FPP 1FT1 1N4Q 1QBQ 1TN6 1TN7 1TNB 1TNO 1TNU 1TNY 1TNZ |
Descriptor | Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit, Protein farnesyltransferase beta subunit, peptide derived from the C-terminus of H-Ras, ... (7 entities in total) |
Functional Keywords | ftase, farnesyltransferase, farnesyl transferase, prenyltransferase, caax, ras, lipid modification, prenylation, substrate selectivity, transferase |
Biological source | Rattus norvegicus (Norway rat) More |
Total number of polymer chains | 3 |
Total formula weight | 93782.86 |
Authors | Reid, T.S.,Terry, K.L.,Casey, P.J.,Beese, L.S. (deposition date: 2004-06-11, release date: 2004-11-02, Last modification date: 2023-08-23) |
Primary citation | Reid, T.S.,Terry, K.L.,Casey, P.J.,Beese, L.S. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J.Mol.Biol., 343:417-433, 2004 Cited by PubMed: 15451670DOI: 10.1016/j.jmb.2004.08.056 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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