EC Number   |
|---|
   2.7.1.105 | hanging drop vapour-diffusion method using PEG 6000 as precipitant. Single crystals are grown in the presence of MgATP and diffracted to 1.98 A. The crystals belong to the orthorhombic system, space group P222(1), with unit-cell parameters a = 42.8, b = 86.8, c = 171.3 A |
| 2.7.1.105 | His-tagged enzyme recombinantly expressed in Escherichia coli, sitting drop vapor diffusion method |
| 2.7.1.105 | oligomeric state observed in the crystal is tetrameric, structural elements involved in the binding of the substrate and allosteric ATPs are also participating in the dimer-dimer interface, data collection parameters and structure refinement statistics |
| 2.7.1.105 | sitting-drop, vapor-diffusion method, crystal structures of PFKFB3/beta,gamma-methylene-adenosine 5'-triphosphate/fructose-6-phosphate and PFKFB3/ADP/phosphoenolpyruvate complexes are determined to 2.7 A and 2.25 A resolution |
| 2.7.1.105 | the crystal structure of H256A to a resolution of 2.4 A by molecular replacement |
| 2.7.1.105 | the crystal structure of liver enzyme: a head-to-head homodimer, depending on the liganding conditions each subunit contains an ATPgammaS, ADP or P molecule to the kinase domain, and two phosphates, regardless of the liganding conditions, bound to phosphatase domain, structure of enzyme very similar to that of the rat testis isoform |
| 2.7.1.105 | the crystal structure of mutant enzyme, the two subunits in the homodimer are arranged in a head-to-head manner, each monomer consists of independent kinase and phosphatase domains, the kinase domains are in close contact, forming an extended hydrophobic core between them, while the phosphatase domains are essentially independent of one another, enzyme is related to the nucleotide monophosphate kinases, and the catalytic domain of G proteins |
| 2.7.1.105 | to 1.8 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ADP, ADP mimicks the catalytic binding mode of ATP |
| 2.7.1.105 | to 2.0 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ATP analogue AMPPNP, the presence of a gamma-phosphate makes adoption of the catalytic ATP binding mode impossible for AMPPNP, forcing the analogue to bind atypically with concomitant conformational changes to the ATP binding-pocket |
