› 1a47

X-ray diffraction
2.56Å resolution

CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR

Released:
DOI: 10.2210/pdb1a47/pdb
PDB entry 1a47 coloured by chain, front view.
PDB entry 1a47 coloured by chain, side view.
PDB entry 1a47 coloured by chain, top view.
Source organism: Thermoanaerobacterium thermosulfurigenes
Primary publication:
Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
Wind RD, Uitdehaag JC, Buitelaar RM, Dijkstra BW, Dijkhuizen L
J Biol Chem 273 5771-9 (1998)
PMID: 9488711

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-150856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Cyclomaltodextrin glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 683 amino acids
Theoretical weight: 75.5 KDa
Source organism: Thermoanaerobacterium thermosulfurigenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P26827 (Residues: 28-710; Coverage: 100%)
Gene name: amyA
Sequence domains:
Structure domains:

Ligands and Environments

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 ADH 1 x ADH
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 73.996Å b: 97.789Å c: 116.263Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.186 0.25
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Protein engineering of bacterial alpha-amylases.
Nielsen et al. (2000)
8 more

4 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
3 more