6R0H
Glycogen Phosphorylase b in complex with 3
Summary for 6R0H
| Entry DOI | 10.2210/pdb6r0h/pdb |
| Descriptor | Glycogen phosphorylase, muscle form, 3-(4-fluorophenyl)-~{N}-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]benzamide, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 98046.90 |
| Authors | Tsagkarakou, S.A.,Koulas, M.S.,Kyriakis, E.,Stravodimos, G.A.,Skamnaki, V.T.,Leonidas, D.D. (deposition date: 2019-03-13, release date: 2019-04-10, Last modification date: 2025-04-09) |
| Primary citation | Fischer, T.,Koulas, S.M.,Tsagkarakou, A.S.,Kyriakis, E.,Stravodimos, G.A.,Skamnaki, V.T.,Liggri, P.G.V.,Zographos, S.E.,Riedl, R.,Leonidas, D.D. High Consistency of Structure-Based Design and X-Ray Crystallography: Design, Synthesis, Kinetic Evaluation and Crystallographic Binding Mode Determination of Biphenyl-N-acyl-beta-d-Glucopyranosylamines as Glycogen Phosphorylase Inhibitors. Molecules, 24:-, 2019 Cited by PubMed Abstract: Structure-based design and synthesis of two biphenyl--acyl-β-d-glucopyranosylamine derivatives as well as their assessment as inhibitors of human liver glycogen phosphorylase (hlGPa, a pharmaceutical target for type 2 diabetes) is presented. X-ray crystallography revealed the importance of structural water molecules and that the inhibitory efficacy correlates with the degree of disturbance caused by the inhibitor binding to a loop crucial for the catalytic mechanism. The in silico-derived models of the binding mode generated during the design process corresponded very well with the crystallographic data. PubMed: 30987252DOI: 10.3390/molecules24071322 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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