› 1q6d

X-ray diffraction
2Å resolution

Crystal structure of Soybean Beta-Amylase Mutant (M51T) with Increased pH Optimum

Released:
DOI: 10.2210/pdb1q6d/pdb
PDB entry 1q6d coloured by chain, front view.
PDB entry 1q6d coloured by chain, side view.
PDB entry 1q6d coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum.
Hirata A, Adachi M, Sekine A, Kang YN, Utsumi S, Mikami B
J Biol Chem 279 7287-95 (2004)
PMID: 14638688

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 495 amino acids
Theoretical weight: 55.94 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: P10538 (Residues: 2-496; Coverage: 100%)
Gene name: BMY1
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P3121
Unit cell:
a: 86.354Å b: 86.354Å c: 145.629Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.215
Expression system: Escherichia coli

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Citations

4 review citations

Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications.
Sharma et al. (2012)
3 more