Activating Compound | Comment | Organism | Structure |
---|---|---|---|
AMP | physiological activator | Oryctolagus cuniculus |
Crystallization (Comment) | Organism |
---|---|
crystal structure of the cocrystallized rabbit muscle glycogen phosphorylase bFR258900 complex, 2.2 A resolution | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
FR258900 | the inhibitor binds at the allosteric activator site, where the physiological activator AMP binds. The contacts from FR258900 to glycogen phosphorylase are dominated by nonpolar van der Waals interactions with Gln71, Gln72, Phe196, and Val459 (from the symmetry-related subunit), and also by ionic interactions from the carboxylate groups to the three arginine residues (Arg242, Arg309, and Arg310) that form the allosteric phosphate-recognition subsite. The binding of FR258900 to the protein promotes conformational changes that stabilize an inactive T-state quaternary conformation of the enzyme | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P00489 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycogen + glucose 1-phosphate | - |
Oryctolagus cuniculus | glycogen + phosphate | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00046 | - |
FR258900 | - |
Oryctolagus cuniculus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0003 | - |
- |
Oryctolagus cuniculus | FR258900 |