1AXR
COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B
Summary for 1AXR
Entry DOI | 10.2210/pdb1axr/pdb |
Descriptor | GLYCOGEN PHOSPHORYLASE, PHOSPHATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total) |
Functional Keywords | transferase, glycosidases, glycogen phosphorylase, catalytic mechanism, azolopyridines, inhibitors |
Biological source | Oryctolagus cuniculus (rabbit) |
Total number of polymer chains | 1 |
Total formula weight | 97930.47 |
Authors | Oikonomakos, N.G.,Heightman, T.D. (deposition date: 1997-10-20, release date: 1998-01-28, Last modification date: 2024-06-05) |
Primary citation | Heightman, T.D.,Vasella, A.,Tsitsanou, K.E.,Zographos, S.E.,Skamnaki, V.T.,Oikonomakos, N.G. Cooperative interactions of the catalytic nucleophile and the catalytic acid in the inhibition of beta-glycosidases. Calculations and their validation by comparative kinetic and structural studies of the inhibition of glycogen phosphorylase b. HELV.CHIM.ACTA, 81:853-864, 1998 Cited by |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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