› 1v3j

X-ray diffraction
2Å resolution

Crystal structure of F283L mutant cyclodextrin glycosyltransferase

Released:
DOI: 10.2210/pdb1v3j/pdb
PDB entry 1v3j coloured by chain, front view.
PDB entry 1v3j coloured by chain, side view.
PDB entry 1v3j coloured by chain, top view.
Source organism: Bacillus sp. 1011
Primary publication:
Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.
Kanai R, Haga K, Akiba T, Yamane K, Harata K
Protein Sci 13 457-65 (2004)
PMID: 14739329

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
Macromolecule:
Cyclomaltodextrin glucanotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 686 amino acids
Theoretical weight: 75.2 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

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P1
Unit cell:
a: 63.93Å b: 73.66Å c: 78.2Å
α: 85.11° β: 104.96° γ: 100.97°
R-values:
R R work R free
0.174 0.17 0.242
Expression system: Escherichia coli

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Citations

1 review citation

Recent advances in discovery, heterologous expression, and molecular engineering of cyclodextrin glycosyltransferase for versatile applications.
Han et al. (2014)
6 other articles

1 mention without citation

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.
Kanai et al. (2004)