EC Number |
---|
2.5.1.60 | - |
2.5.1.60 | at 2.0 Angstrom resolution, the beta subunit forms an alpha-alpha barrel that contains most of the residues in the active site, the alpha subunit consists of a helical domain, an immunoglobulin-like domain and a leucine-rich repeat domain, the N-terminal alpha subunit binds to the active site in the beta subunit |
2.5.1.60 | at 2.7 Angstom, crystal structure of REP-1 in complex with farnesyl-loaded enzyme, contact between the two proteins is formed through domain II of REP-1 and the alpha subunit of the enzyme |
2.5.1.60 | enzyme-inhibitor complex with an engeneered enzyme lacking the LRR- and Ig-domains, complexes are prepared by soaking of co-crystallization, diffraction data collection at -173°C |
2.5.1.60 | in complex with geranylgeranyl diphosphate, hanging drop vapour diffusion method, with 14% (w/v) PEG 3350, 0.2M CaAc2, 0.1 M HEPES pH 7.2 |
2.5.1.60 | structure of the full-length GGTase3-FBXL2-SKP1 complex reveals an extensive multivalent interface specifically formed between the leucine-rich repeat domain of substrate FBXL2 and subunit PTAR1 |