4AIO: Crystal Structure Of The Starch Debranching Enzyme Barley Limit Dextrinase

Citation:
Abstract
Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 A 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 alpha-cyclodextrin and beta-cyclodextrin solved to 2.5 and 2.1 A 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.
PDB ID: 4AIODownload
MMDB ID: 101961
PDB Deposition Date: 2012/2/11
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 4AIO: monomeric; determined by author and by software (PISA)
Molecular Components in 4AIO
Label Count Molecule
Protein (1 molecule)
1
Limit Dextrinase
Molecule annotation
Chemicals (10 molecules)
1
4
2
2
3
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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