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X-ray diffraction
1.5Å resolution

Crystal structure of Bacillus sp. AHU2216 GH13_31 Alpha-glucosidase E256Q/N258P in complex with maltotriose

Released:
DOI: 10.2210/pdb8ids/pdb
PDB entry 8ids coloured by chain, front view.
PDB entry 8ids coloured by chain, side view.
PDB entry 8ids coloured by chain, top view.
Source organism: Bacillus sp. (in: Bacteria)
Primary publication:
Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5.
Auiewiriyanukul W, Saburi W, Ota T, Yu J, Kato K, Yao M, Mori H
OpenAccess logo Molecules 28 (2023)
PMID: 37049872

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycosyl hydrolase family 13 catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 563 amino acids
Theoretical weight: 65.98 KDa
Source organism: Bacillus sp. (in: Bacteria)
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2Z5WH92 (Residues: 1-555; Coverage: 100%)
Gene name: BspAG13A
Sequence domains:

Ligands and Environments

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
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 56.517Å b: 89.202Å c: 128.282Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.186
Expression system: Escherichia coli

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Citations

1 mention without citation

Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5.
Auiewiriyanukul et al. (2023)