Summary for 1ABE
| Entry DOI | 10.2210/pdb1abe/pdb |
| Descriptor | L-ARABINOSE-BINDING PROTEIN, alpha-L-arabinopyranose, beta-L-arabinopyranose, ... (4 entities in total) |
| Functional Keywords | binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 33551.26 |
| Authors | Vyas, N.K.,Quiocho, F.A. (deposition date: 1992-04-23, release date: 1993-10-31, Last modification date: 2024-02-07) |
| Primary citation | Quiocho, F.A.,Vyas, N.K. Novel stereospecificity of the L-arabinose-binding protein Nature, 310:381-386, 1984 Cited by PubMed Abstract: Tertiary structure refinement at 1.7 A resolution of the liganded form of L-arabinose-binding protein from Escherichia coli has revealed a novel binding site geometry which accommodates both alpha- and beta-anomers of L-arabinose. This detailed structure analysis provides new understanding of protein-sugar interaction, the process by which the binding protein minimizes the difference in the stability of the two bound sugar anomers, and the roles of periplasmic binding proteins in active transport. PubMed: 6379466DOI: 10.1038/310381a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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