› 1ukp

X-ray diffraction
2.1Å resolution

Crystal structure of soybean beta-amylase mutant substituted at surface region

Released:
DOI: 10.2210/pdb1ukp/pdb
PDB entry 1ukp coloured by chain, front view.
PDB entry 1ukp coloured by chain, side view.
PDB entry 1ukp coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Change in the crystal packing of soybean beta-amylase mutants substituted at a few surface amino acid residues.
Kang YN, Adachi M, Mikami B, Utsumi S
Protein Eng 16 809-17 (2003)
PMID: 14631070

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 495 amino acids
Theoretical weight: 56.03 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 20 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P1
Unit cell:
a: 75.463Å b: 78.801Å c: 88.56Å
α: 89.92° β: 90.21° γ: 89.9°
R-values:
R R work R free
0.2 0.2 0.234
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.
Yang et al. (2004)
1 more