4KC1
Structure of the blood group glycosyltransferase AAglyB in complex with a pyridine inhibitor as a neutral pyrophosphate surrogate
Summary for 4KC1
| Entry DOI | 10.2210/pdb4kc1/pdb |
| Related | 4KC2 4KC4 |
| Descriptor | Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, MANGANESE (II) ION, octyl 2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-galactopyranoside, ... (5 entities in total) |
| Functional Keywords | gta superfanily, blood group proteins, glycosyltransferase, fuc-gal, adp-gal, adp-galnac, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein: P16442 |
| Total number of polymer chains | 1 |
| Total formula weight | 34768.94 |
| Authors | Cuesta-Seijo, J.A.,Wang, S.,Lafont, D.,Vidal, S.,Palcic, M.M. (deposition date: 2013-04-24, release date: 2013-09-11, Last modification date: 2023-09-20) |
| Primary citation | Wang, S.,Cuesta-Seijo, J.A.,Lafont, D.,Palcic, M.M.,Vidal, S. Design of glycosyltransferase inhibitors: pyridine as a pyrophosphate surrogate. Chemistry, 19:15346-15357, 2013 Cited by PubMed Abstract: A series of ten glycosyltransferase inhibitors has been designed and synthesized by using pyridine as a pyrophosphate surrogate. The series was prepared by conjugation of carbohydrate, pyridine, and nucleoside building blocks by using a combination of glycosylation, the Staudinger-Vilarrasa amide-bond formation, and azide-alkyne click chemistry. The compounds were evaluated as inhibitors of five metal-dependent galactosyltransferases. Crystallographic analyses of three inhibitors complexed in the active site of one of the enzymes confirmed that the pyridine moiety chelates the Mn(2+) ion causing a slight displacement (2 Å) from its original position. The carbohydrate head group occupies a different position than in the natural uridine diphosphate (UDP)-Gal substrate with little interaction with the enzyme. PubMed: 24108680DOI: 10.1002/chem.201301871 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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