4AIO
Crystal structure of the starch debranching enzyme barley limit dextrinase
Summary for 4AIO
| Entry DOI | 10.2210/pdb4aio/pdb |
| Descriptor | LIMIT DEXTRINASE, GLYCEROL, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, pullulanase, glycoside hydrolase family 13 |
| Biological source | HORDEUM VULGARE (BARLEY) |
| Total number of polymer chains | 1 |
| Total formula weight | 98400.30 |
| Authors | Moeller, M.S.,Abou Hachem, M.,Svensson, B.,Henriksen, A. (deposition date: 2012-02-11, release date: 2012-08-15, Last modification date: 2023-12-20) |
| Primary citation | Moeller, M.S.,Abou Hachem, M.,Svensson, B.,Henriksen, A. Structure of the Starch-Debranching Enzyme Barley Limit Dextrinase Reveals Homology of the N-Terminal Domain to Cbm21. Acta Crystallogr.,Sect.F, 68:1008-, 2012 Cited by PubMed Abstract: Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses α-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 Å resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of HvLD in complex with the competitive inhibitors α-cyclodextrin and β-cyclodextrin solved to 2.5 and 2.1 Å resolution, respectively. However, three loops in the N-terminal domain that are shown here to resemble carbohydrate-binding module family 21 were traceable and were included in the present HvLD structure but were too flexible to be traced and included in the structures of the two HvLD-inhibitor complexes. PubMed: 22949184DOI: 10.1107/S1744309112031004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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