› 1b1y

X-ray diffraction
2.5Å resolution

SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE

Released:
DOI: 10.2210/pdb1b1y/pdb
PDB entry 1b1y coloured by chain, front view.
PDB entry 1b1y coloured by chain, side view.
PDB entry 1b1y coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution.
Mikami B, Yoon HJ, Yoshigi N
J Mol Biol 285 1235-43 (1999)
PMID: 9918723

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-147608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 56.32 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: P16098 (Residues: 5-504; Coverage: 94%)
Gene names: AMYB, BMY1
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 72.11Å b: 72.11Å c: 250.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.256
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Starch: its metabolism, evolution, and biotechnological modification in plants.
Zeeman et al. (2010)
1 more

2 mentions without citation

SuperSite: dictionary of metabolite and drug binding sites in proteins.
Bauer et al. (2009)
1 more