› 3ede

X-ray diffraction
1.71Å resolution

Structural base for cyclodextrin hydrolysis

Released:
DOI: 10.2210/pdb3ede/pdb
PDB entry 3ede coloured by chain, front view.
PDB entry 3ede coloured by chain, side view.
PDB entry 3ede coloured by chain, top view.
Source organism: Flavobacterium sp. 92
Primary publication:
Structural base for enzymatic cyclodextrin hydrolysis.
Buedenbender S, Schulz GE
J Mol Biol 385 606-17 (2009)
PMID: 19014948

Function and Biology Details

Reaction catalysed: 
Cyclomaltodextrin + H(2)O = linear maltodextrin
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185144 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 13 catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 601 amino acids
Theoretical weight: 68.02 KDa
Source organism: Flavobacterium sp. 92
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KKG0 (Residues: 19-619; Coverage: 100%)
Gene name: cdase
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 106.355Å b: 111.036Å c: 106.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.202
Expression system: Escherichia coli

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Citations

6 review citations

Cyclodextrins.
Kurkov et al. (2013)
5 more