EC Number   |
Reference |
|---|
    2.7.1.2 | 1.85 A resolution X-ray crystal structure of the apo form |
759749 |
| 2.7.1.2 | crystal structures in complexes with inhibitors 2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose, 2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose. The analogues all share a common glucose moietythat preserves key enzyme-substrate hydrogen bonding interactions with the monosaccharide hydroxyl groups from C1, C3, C4,and C6. The C2 hydroxyl is replaced by a NH group and also par-ticipates in the key hydrogen bonding |
739028 |
| 2.7.1.2 | crystal structures of apo-SgGlkA, SgGlkA in complex with glucose, and SgGlkA in complex with glucose and adenylyl imidodiphosphate (AMPPNP) are reported. SgGlkA is divided into a small alpha/beta domain and a large alpha + beta domain, and it forms a dimer-of-dimer tetrameric configuration |
722553 |
| 2.7.1.2 | crystallized using the sitting-drop vapour-diffusion method. A crystal of SgGlkA in complex with glucose is obtained and diffracted X-rays to 1.84 A resolution |
721213 |
| 2.7.1.2 | crystals of TcGlcK in complex with D-glucose and ADP are obtained by the hanging-drop, vapor-diffusion method, using PEG3350 as precipitant agent and diammonium hydrogen citrate as additive. A complete native dataset is collected to 2.1 A maximum resolution |
688372 |
| 2.7.1.2 | homology modeling of structure. Staphylococcus aureus glucokinase exhibits very close homology with Enterococcus faecalis and Clostridium difficle while with other bacteria it show a high degree of variations both in domain and nondomain regions. Glucose interacts with residues V77, N114, S161 and G160 forming a total of eight hydrogen bonds. Glucose docking score is -12.3697 kcal/mol |
738362 |
| 2.7.1.2 | purified recombinant selenomethionine-labeled enzyme free or in complex with D-glucose, hanging drop vapour diffusion method, 0.002 ml enzyme solution containing 6.8 mg/ml protein mixed with 0.004 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 1.7 M ammonium sulfate for the apo-enzyme or 18.5-20% PEG 6000 with 2 mM D-glucose and 2-3 mM ADP for the glucose-bound enzyme, X-ray diffraction structure determination and analysis at 2.3-2.2 A resolution |
662022 |
| 2.7.1.2 | the enzyme is crystallized in an apo form. Sitting-drop vapor diffusion at room temperature |
759365 |
| 2.7.1.2 | the structure is determined and refined to 2.2 A resolution |
758654 |
