› 2y5e

X-ray diffraction
2.49Å resolution

BARLEY LIMIT DEXTRINASE IN COMPLEX WITH ALPHA-CYCLODEXTRIN

Released:
DOI: 10.2210/pdb2y5e/pdb
PDB entry 2y5e coloured by chain, front view.
PDB entry 2y5e coloured by chain, side view.
PDB entry 2y5e coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins.
Vester-Christensen MB, Abou Hachem M, Svensson B, Henriksen A
J Mol Biol 403 739-50 (2010)
PMID: 20863834

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Limit dextrinase Chain: A
Molecule details ›
Chain: A
Length: 884 amino acids
Theoretical weight: 97.44 KDa
Source organism: Hordeum vulgare
Expression system: Komagataella phaffii GS115
UniProt:
  • Canonical: O48541 (Residues: 22-503, 505-904; Coverage: 98%)
Gene name: HvLD99
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand GOL 1 x GOL
Ligand CA 2 x CA
Ligand IOD 8 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-5
Spacegroup: C2
Unit cell:
a: 174.84Å b: 85.61Å c: 61.12Å
α: 90° β: 96.83° γ: 90°
R-values:
R R work R free
0.175 0.175 0.226
Expression system: Komagataella phaffii GS115

Quick links

Citations

5 review citations

Proteomes of the barley aleurone layer: A model system for plant signalling and protein secretion.
Finnie et al. (2011)
4 more

1 mention without citation

Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.
Møller et al. (2012)