› 4aio

X-ray diffraction
1.9Å resolution

Crystal structure of the starch debranching enzyme barley limit dextrinase

Released:
DOI: 10.2210/pdb4aio/pdb
PDB entry 4aio coloured by chain, front view.
PDB entry 4aio coloured by chain, side view.
PDB entry 4aio coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.
Møller MS, Abou Hachem M, Svensson B, Henriksen A
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 1008-12 (2012)
PMID: 22949184

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
Macromolecule:
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

3 bound ligands:
Ligand GOL 4 x GOL
Ligand CA 2 x CA
Ligand IOD 4 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 176.058Å b: 82.072Å c: 59.378Å
α: 90° β: 96.2° γ: 90°
R-values:
R R work R free
0.189 0.187 0.225
Expression system: Komagataella phaffii GS115

Quick links

Citations

2 review citations

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

4 mentions without citation

Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors.
Møller et al. (2015)
3 more