› 1cxe

X-ray diffraction
2.1Å resolution

COMPLEX OF CGTASE WITH MALTOTETRAOSE AT ROOM TEMPERATURE AND PH 9.1 BASED ON DIFFRACTION DATA OF A CRYSTAL SOAKED WITH ALPHA-CYCLODEXTRIN

Released:
DOI: 10.2210/pdb1cxe/pdb
PDB entry 1cxe coloured by chain, front view.
PDB entry 1cxe coloured by chain, side view.
PDB entry 1cxe coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
Knegtel RM, Strokopytov B, Penninga D, Faber OG, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW
J Biol Chem 270 29256-64 (1995)
PMID: 7493956

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-155054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Cyclomaltodextrin glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 686 amino acids
Theoretical weight: 74.58 KDa
Source organism: Niallia circulans
UniProt:
  • Canonical: P43379 (Residues: 28-713; Coverage: 100%)
Gene name: cgt
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 121.388Å b: 111.604Å c: 66.386Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 not available 0.1

Quick links

Citations

13 review citations

Properties and applications of starch-converting enzymes of the alpha-amylase family.
van der Maarel et al. (2002)
12 more

2 mentions without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)
1 more