EC Number   |
|---|
   1.14.11.67 | JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution |
| 1.14.11.67 | N-terminal fragments of the enzyme in complex with inhibitors, sitting drop vapor diffusion method, using 1.2-1.35 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.6-9.2), 0-20% (v/v) glycerol and 25 mM (Na/K) dibasic/monobasic phosphate |
| 1.14.11.67 | purified recombinant enzyme in complex with inhibitor KDOAM-25, sitting drop vapor diffusion method, mixing of 50 nl of 8.1 mg/ml protein in solution with 1 mM KDOAM-25 and 4 mM MnCl2, is mixed with ,precipitant solution consisting of 1.6 M Na/K phosphate, and 0.1 M HEPES, pH 7.5, and 20 nL of KDM5B seeds of crystals obtained from the same condition, 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling |
| 1.14.11.67 | purified recombinant enzyme, free or in complex with N-oxalylglycine, X-ray diffraction structure determination and analysis at 2.35 A resolution |
| 1.14.11.67 | solution strucuture of apo and H3-bound domain PHD1. The H3 peptide adopts a helical conformation that allows for extended interactions between the H3 ligand and PHD1 reader domain. H3 residues A1, R2, and K4 are the major determinants of H3 peptide binding, with smaller contributions from H3T3 |
| 1.14.11.67 | structure of intact multi-domain KDM5B. The PLU region, in the central region of KDM5B, has a curved alpha-helical three-dimensional structure that acts as a rigid linker between the catalytic core and a region comprising four alpha-helices, a loop comprising the PHD2 domain, two large intrinsically disordered loops and the PHD3 domain in close proximity. The dumbbell shaped and curved KDM5B architecture is complementary to the nucleosome surface and has a striking overall similarity to that of the functionally related KDM1A/CoREST complex |
