5MEM
A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe.
Summary for 5MEM
| Entry DOI | 10.2210/pdb5mem/pdb |
| Descriptor | Glycogen phosphorylase, muscle form, PYRIDOXAL-5'-PHOSPHATE, 2-[[1-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]-2-oxidanylidene-pyrimidin-4-yl]amino]-10~{H}-acridin-9-one, ... (4 entities in total) |
| Functional Keywords | gp inhibitors, glucopyranosyl cytosine acridine derivatives, electronic absorption spectra, fluorescence spectra, fluorescent protein |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 98135.98 |
| Authors | Mamais, M.,Chrysina, E.D. (deposition date: 2016-11-15, release date: 2017-11-29, Last modification date: 2025-04-09) |
| Primary citation | Mamais, M.,Degli Esposti, A.,Kouloumoundra, V.,Gustavsson, T.,Monti, F.,Venturini, A.,Chrysina, E.D.,Markovitsi, D.,Gimisis, T. A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site. Chemistry, 23:8800-8805, 2017 Cited by PubMed Abstract: The design and synthesis of a glucose-based acridone derivative (GLAC), a potent inhibitor of glycogen phosphorylase (GP) are described. GLAC is the first inhibitor of glycogen phosphorylase, the electronic absorption properties of which are clearly distinguishable from those of the enzyme. This allows probing subtle interactions in the catalytic site. The GLAC absorption spectra, associated with X-ray crystallography and quantum chemistry calculations, reveal that part of the catalytic site of GP behaves as a highly basic environment in which GLAC exists as a bis-anion. This is explained by water-bridged hydrogen-bonding interactions with specific catalytic site residues. PubMed: 28493496DOI: 10.1002/chem.201701591 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
Download full validation report
