6RQK
Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole
Summary for 6RQK
| Entry DOI | 10.2210/pdb6rqk/pdb |
| Descriptor | Alpha-1,6-mannosidase, (5R,6R,7S,8R)-5-(HYDROXYMETHYL)-5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL (3 entities in total) |
| Functional Keywords | carbohydrate, inhibitor, glycoside hydrolase, complex, hydrolase |
| Biological source | Clostridium perfringens str. 13 |
| Total number of polymer chains | 2 |
| Total formula weight | 102524.75 |
| Authors | Males, A.,Davies, G.J. (deposition date: 2019-05-16, release date: 2019-08-28, Last modification date: 2024-01-24) |
| Primary citation | Males, A.,Speciale, G.,Williams, S.J.,Davies, G.J. Distortion of mannoimidazole supports a B2,5boat transition state for the family GH125 alpha-1,6-mannosidase from Clostridium perfringens. Org.Biomol.Chem., 17:7863-7869, 2019 Cited by PubMed Abstract: Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 α-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family. PubMed: 31407758DOI: 10.1039/c9ob01161g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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