› 2dij

X-ray diffraction
2.6Å resolution

COMPLEX OF A Y195F MUTANT CGTASE FROM B. CIRCULANS STRAIN 251 COMPLEXED WITH A MALTONONAOSE INHIBITOR AT PH 9.8 OBTAINED AFTER SOAKING THE CRYSTAL WITH ACARBOSE AND MALTOHEXAOSE

Released:
DOI: 10.2210/pdb2dij/pdb
PDB entry 2dij coloured by chain, front view.
PDB entry 2dij coloured by chain, side view.
PDB entry 2dij coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
Strokopytov B, Knegtel RM, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW
Biochemistry 35 4241-9 (1996)
PMID: 8672460

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 (6 distinct):
Cyclomaltodextrin glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 686 amino acids
Theoretical weight: 74.56 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
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
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, G6D
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand CA 2 x CA
Ligand ADH 1 x ADH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 119.964Å b: 111.282Å c: 67.977Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Structural and sequence-based classification of glycoside hydrolases.
Henrissat et al. (1997)
7 more

3 mentions without citation

Evolution of Protein Structure and Stability in Global Warming.
Barik S. (2020)
2 more