› 1i75

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN

Released:
DOI: 10.2210/pdb1i75/pdb
PDB entry 1i75 coloured by chain, front view.
PDB entry 1i75 coloured by chain, side view.
PDB entry 1i75 coloured by chain, top view.
Source organism: Bacillus sp. (in: Bacteria)
Primary publication:
Crystal structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 complexed with 1-deoxynojirimycin at 2.0 A resolution.
Kanai R, Haga K, Yamane K, Harata K
J Biochem 129 593-8 (2001)
PMID: 11275559

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-529319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclomaltodextrin glucanotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 686 amino acids
Theoretical weight: 75.23 KDa
Source organism: Bacillus sp. (in: Bacteria)
Expression system: Escherichia coli
UniProt:
  • Canonical: P05618 (Residues: 28-713; Coverage: 100%)
Gene name: cgt
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand NOJ 4 x NOJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P1
Unit cell:
a: 64.78Å b: 74.24Å c: 79.03Å
α: 85.03° β: 104.88° γ: 101.02°
R-values:
R R work R free
0.154 0.154 0.214
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

2 mentions without citation

Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine Bacterium Saccharophagus degradans 2-40 T.
Ding et al. (2021)
1 more