5FOO
6-phospho-beta-glucosidase
Summary for 5FOO
Entry DOI | 10.2210/pdb5foo/pdb |
Descriptor | 6-PHOSPHO-BETA-D GLYCOSIDASE, 6-PHOSPHOCYCLOPHELLITOL, 1,2-ETHANEDIOL, ... (7 entities in total) |
Functional Keywords | hydrolase, glycoside hydrolase, cyclophellitol, glucose 6-phosphate |
Biological source | STREPTOCOCCUS PYOGENES |
Total number of polymer chains | 6 |
Total formula weight | 334538.79 |
Authors | Jin, Y.,Kwan, D.H.,Withers, S.G.,Davies, G.J. (deposition date: 2015-11-24, release date: 2016-02-17, Last modification date: 2024-01-10) |
Primary citation | Kwan, D.H.,Jin, Y.,Jiang, J.,Chen, H.,Kotzler, M.P.,Overkleeft, H.S.,Davies, G.J.,Withers, S.G. Chemoenzymatic Synthesis of 6-Phospho-Cyclophellitol as a Novel Probe of 6-Phospho-Beta-Glucosidases. FEBS Lett., 590:461-, 2016 Cited by PubMed Abstract: Covalent, mechanism-based inhibitors of glycosidases are valuable probe molecules for visualizing enzyme activities in complex systems. We, here, describe the chemoenzymatic synthesis of 6-phospho-cyclophellitol and evaluate its behaviour as a mechanism-based inactivator of the Streptococcus pyogenes 6-phospho-β-glucosidase from CAZy family GH1. We further present the three-dimensional structure of the inactivated enzyme, which reveals the constellation of active site residues responsible for the enzyme's specificity and confirms the covalent nature of the inactivation. PubMed: 26790390DOI: 10.1002/1873-3468.12059 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report