› 1ukt

X-ray diffraction
2.2Å resolution

Crystal structure of Y100L mutant cyclodextrin glucanotransferase compexed with an acarbose

Released:
DOI: 10.2210/pdb1ukt/pdb
PDB entry 1ukt coloured by chain, front view.
PDB entry 1ukt coloured by chain, side view.
PDB entry 1ukt coloured by chain, top view.
Source organism: Bacillus sp. 1011
Primary publication:
Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011.
Haga K, Kanai R, Sakamoto O, Aoyagi M, Harata K, Yamane K
J Biochem 134 881-91 (2003)
PMID: 14769878

Function and Biology Details

Reaction catalysed: 
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Cyclomaltodextrin glucanotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 686 amino acids
Theoretical weight: 75.18 KDa
Source organism: Bacillus sp. 1011
Expression system: Escherichia coli
UniProt:
  • Canonical: P05618 (Residues: 28-713; Coverage: 100%)
Gene name: cgt
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GAL, GLC, GLD
Carbohydrate polymer
2 bound ligands:
Ligand ACI 2 x ACI
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 65.68Å b: 74.47Å c: 80.1Å
α: 85.29° β: 105.59° γ: 100.81°
R-values:
R R work R free
0.179 0.173 0.276
Expression system: Escherichia coli

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Citations

2 review citations

Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.
Leemhuis et al. (2010)
1 more