› 4j3v

X-ray diffraction
1.45Å resolution

Crystal structure of barley limit dextrinase in complex with a branched thio-linked hexasaccharide

Released:
DOI: 10.2210/pdb4j3v/pdb
PDB entry 4j3v coloured by chain, front view.
PDB entry 4j3v coloured by chain, side view.
PDB entry 4j3v coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase.
Møller MS, Windahl MS, Sim L, Bøjstrup M, Abou Hachem M, Hindsgaul O, Palcic M, Svensson B, Henriksen A
J Mol Biol 427 1263-1277 (2015)
PMID: 25562209

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-190388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 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
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, SGD
Ligand GLC 5 x GLC
Ligand SGD 1 x SGD
3 bound ligands:
Ligand IOD 9 x IOD
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: C2
Unit cell:
a: 173.99Å b: 85.82Å c: 61.55Å
α: 90° β: 95.98° γ: 90°
R-values:
R R work R free
0.136 0.134 0.169
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structure and function of α-glucan debranching enzymes.
Møller et al. (2016)
3 more