› 3gbd

X-ray diffraction
1.95Å resolution

Crystal structure of the isomaltulose synthase SmuA from Protaminobacter rubrum

Released:
DOI: 10.2210/pdb3gbd/pdb
PDB entry 3gbd coloured by chain, front view.
PDB entry 3gbd coloured by chain, side view.
PDB entry 3gbd coloured by chain, top view.
Source organism: Serratia plymuthica
Primary publication:
Structural determinants of product specificity of sucrose isomerases.
Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, Aghajari N
FEBS Lett 583 1964-8 (2009)
PMID: 19427862

Function and Biology Details

Reaction catalysed: 
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 13 catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 558 amino acids
Theoretical weight: 65.69 KDa
Source organism: Serratia plymuthica
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VX20 (Residues: 1-558; Coverage: 100%)
Gene name: smuA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 8 x EDO
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 61.63Å b: 81.39Å c: 135.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.224
Expression system: Escherichia coli

Quick links

Citations

3 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
2 more

3 mentions without citation

Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.
Sardiña-Peña et al. (2023)
2 more