› 1byd

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

Released:
DOI: 10.2210/pdb1byd/pdb
PDB entry 1byd coloured by chain, front view.
PDB entry 1byd coloured by chain, side view.
PDB entry 1byd coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis.
Mikami B, Degano M, Hehre EJ, Sacchettini JC
Biochemistry 33 7779-87 (1994)
PMID: 8011643

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 (2 distinct):
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 495 amino acids
Theoretical weight: 56.07 KDa
Source organism: Glycine max
Expression system: Not provided
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: RR7, GLC
Carbohydrate polymer
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 86.2Å b: 86.2Å c: 144.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 0.145 not available
Expression system: Not provided

Quick links

Citations

9 review citations

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

2 mentions without citation

Molecular mimicry of substrate oxygen atoms by water molecules in the beta-amylase active site.
Pujadas et al. (2001)
1 more