› 5cgt

X-ray diffraction
2.5Å resolution

MALTOTRIOSE COMPLEX OF PRECONDITIONED CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT

Released:
DOI: 10.2210/pdb5cgt/pdb
PDB entry 5cgt coloured by chain, front view.
PDB entry 5cgt coloured by chain, side view.
PDB entry 5cgt coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production.
Parsiegla G, Schmidt AK, Schulz GE
Eur J Biochem 255 710-7 (1998)
PMID: 9738912

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-151845 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Cyclomaltodextrin glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 684 amino acids
Theoretical weight: 74.52 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P30920 (Residues: 35-718; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
2 bound ligands:
Ligand GLC 1 x GLC
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 93.5Å b: 104.9Å c: 113.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.247
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
7 more

1 mention without citation

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