CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
The structure was published by Long, S.B., Casey, P.J., and Beese, L.S., in 2000 in a paper entitled "The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely farnesyltransferase (alpha subunit), farnesyltransferase (beta subunit), and K-RAS4B PEPTIDE SUBSTRATE.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms heterotrimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 3 unique UniProt proteins: