EC Number   |
Reference |
|---|
    2.7.1.147 | 2.3 A resolution, R-factor of 20.4% |
395241 |
| 2.7.1.147 | crystal structures of apo form and holo form, in the presence of D-glucose and the nonhydrolyzable ADP analog adenosine 5'-(3-thio)diphosphate. The conformational changes upon sequential substrate binding can be explained by an almost pure rotation (or a rotation plus a translation) facilitated by residues in the flexible inter-domain connection |
728613 |
| 2.7.1.147 | crystallized with ADP and Mg2+, the structure is determined by multiple isomorphous replacement with anomalous scattering and refined at 2.3 A. Crystals are grown at 25°C by the hanging drop vapor diffusion method |
746520 |
| 2.7.1.147 | enzyme in complex with AMP, sitting drop vapour diffusion method, 10 mg/ml protein in 6 mM ADP-beta-S, 30 mM glucose mixed in equal volumes with reservoir solution containing 1.6 M citrate, pH 6.5, 10 mM DTT, equilibration against 0.075 ml of reservoir solution at 25°C, a few weeks to 1 month, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement, modeling |
662610 |
| 2.7.1.147 | molecular modeling of structure. for binding of ADP, residues M347, I431 and L441 create a hydrophobic pocket around the adenine group. R194 makes a hydrogen bond with alpha and beta phosphates, carbonyl and NH groups from V432 peptide bond make a hydrogen bond with the NH2 group of C6 and the N1 atom of adenine |
727486 |
| 2.7.1.147 | purified enzyme mutant E72A, hanging drop vapor diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 25 mM HEPES/NaOH, pH 7.8, 30 mM MgCl2, 20 mM fructose 6-phosphate, and 20 mM AMP with 0.002 ml of reservoir solution containing 18% PEG 3350 and 0.15 M NaI, 3 days at 18°C, X-ray diffraction structure determination and analysis at 2.61 A resolution, molecular replacement using the structure of Pyrococcus horikoshii ADP-PFK (PDB ID 3DRW) split into small and large domains as search models |
761465 |
| 2.7.1.147 | purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models |
761158 |
| 2.7.1.147 | purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 2.86 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models |
761158 |
| 2.7.1.147 | purified recombinant N-terminally His-tagged apoenzyme, hanging drop vapour diffusion method, 20°C, 10 mg/ml protein in solution is mixed with an equal volume of 0.003 ml of mother liquor containing 9-13% PEG 6000, 0.2 M Li2SO4, and 0.1 M citrate buffer, pH 3.6, heavy atom derivatization with HgCl2, X-ray diffraction structure determination and analysis at 2.0 A resolution, single isomorphous replacement with an anomalous scattering |
663324 |
| 2.7.1.147 | sitting drop vapor diffusion method at 20°C, complex of the enzyme with glucose and 8-bromoadenosine phosphate |
761480 |
