3BSH
Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose
Summary for 3BSH
| Entry DOI | 10.2210/pdb3bsh/pdb |
| Related | 1HT6 3BSG |
| Descriptor | Alpha-amylase type A isozyme, beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | barley alpha-amylase, amy1, mutant, acarbose, complex, calcium, carbohydrate metabolism, germination, glycosidase, hydrolase, metal-binding, secreted |
| Biological source | Hordeum vulgare (Barley) |
| Cellular location | Secreted, extracellular space: P00693 |
| Total number of polymer chains | 1 |
| Total formula weight | 45613.20 |
| Authors | Aghajari, N.,Robert, X.,Haser, R. (deposition date: 2007-12-24, release date: 2008-08-26, Last modification date: 2023-11-01) |
| Primary citation | Nielsen, M.M.,Seo, E.S.,Bozonnet, S.,Aghajari, N.,Robert, X.,Haser, R.,Svensson, B. Multi-site substrate binding and interplay in barley alpha-amylase 1 Febs Lett., 582:2567-2571, 2008 Cited by PubMed Abstract: Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and Y105A/Y380M show that each of Tyr380 and Tyr105 is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr105 predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants. PubMed: 18588886DOI: 10.1016/j.febslet.2008.06.027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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