› 1wdp

X-ray diffraction
1.27Å resolution

The role of an inner loop in the catalytic mechanism of soybean beta-amylase

Released:
DOI: 10.2210/pdb1wdp/pdb
PDB entry 1wdp coloured by chain, front view.
PDB entry 1wdp coloured by chain, side view.
PDB entry 1wdp coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism.
Kang YN, Tanabe A, Adachi M, Utsumi S, Mikami B
Biochemistry 44 5106-16 (2005)
PMID: 15794648

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
Macromolecule:
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 495 amino acids
Theoretical weight: 55.97 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

1 bound ligand:
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3121
Unit cell:
a: 84.888Å b: 84.888Å c: 143.397Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.118 not available 0.174
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts.
Fulton et al. (2008)
11 more

3 mentions without citation

A force field for virtual atom molecular mechanics of proteins.
Korkut et al. (2009)
2 more