Crystallization (Comment) | Organism |
---|---|
in complex with inhibitors beta-D-glucopyranosyl 1-oxalylamide, beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide, beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide. Inhibitors accomodate at the catalytic site at approximately the position of alpha-D-glucose and stabilize the T-state conformation | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide | competitive | Oryctolagus cuniculus | |
beta-D-glucopyranosyl 1-(ethoxy(oxo)acetyl)-amide | competitive | Oryctolagus cuniculus | |
beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide | competitive | Oryctolagus cuniculus | |
beta-D-glucopyranosyl 1-oxalylamide | competitive | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.21 | - |
beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide | - |
Oryctolagus cuniculus | |
0.71 | - |
beta-D-glucopyranosyl 1-oxalylamide | - |
Oryctolagus cuniculus | |
0.92 | - |
beta-D-glucopyranosyl 1-(ethoxy(oxo)acetyl)-amide | - |
Oryctolagus cuniculus | |
1 | - |
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide | - |
Oryctolagus cuniculus |