› 2vdt

X-ray diffraction
3.2Å resolution

Crystallographic structure of Levansucrase from Bacillus subtilis mutant S164A

Released:
DOI: 10.2210/pdb2vdt/pdb
PDB entry 2vdt coloured by chain, front view.
PDB entry 2vdt coloured by chain, side view.
PDB entry 2vdt coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Selected mutations in Bacillus subtilis levansucrase semi-conserved regions affecting its biochemical properties.
Ortiz-Soto ME, Rivera M, Rudiño-Piñera E, Olvera C, López-Munguía A
Protein Eng Des Sel 21 589-95 (2008)
PMID: 18596022

Function and Biology Details

Reaction catalysed: 
Sucrose + (6)-beta-D-fructofuranosyl-(2->)(n) alpha-D-glucopyranoside = glucose + (6)-beta-D-fructofuranosyl-(2->)(n+1) alpha-D-glucopyranoside
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Levansucrase Chain: A
Molecule details ›
Chain: A
Length: 439 amino acids
Theoretical weight: 49.41 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P05655 (Residues: 34-472; Coverage: 99%)
Gene names: BSU34450, sacB
Sequence domains: Levansucrase/Invertase
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: P212121
Unit cell:
a: 50.88Å b: 55.8Å c: 124.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.264 0.297
Expression system: Escherichia coli BL21

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Citations

3 review citations

Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications.
Lammens et al. (2009)
2 more

1 mention without citation

On the use of logarithmic scales for analysis of diffraction data.
Urzhumtsev et al. (2009)