4j3t

X-ray diffraction
1.6Å resolution

Crystal structure of barley Limit dextrinase co-crystallized with 25mM maltotetraose

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Limit dextrinase Chain: A
Molecule details ›
Chain: A
Length: 905 amino acids
Theoretical weight: 99.75 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FYY0 (Residues: 22-905; Coverage: 98%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: C2
Unit cell:
a: 175.09Å b: 86.23Å c: 61.51Å
α: 90° β: 95.58° γ: 90°
R-values:
R R work R free
0.135 0.132 0.177
Expression system: Escherichia coli