› 5i3d

X-ray diffraction
2.16Å resolution

Sulfolobus solfataricus beta-glycosidase - E387Y mutant

Released:
DOI: 10.2210/pdb5i3d/pdb
PDB entry 5i3d coloured by chain, front view.
PDB entry 5i3d coloured by chain, side view.
PDB entry 5i3d coloured by chain, top view.
Source organism: Saccharolobus solfataricus P2
Primary publication:
A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.
Iglesias-Fernández J, Hancock SM, Lee SS, Khan M, Kirkpatrick J, Oldham NJ, McAuley K, Fordham-Skelton A, Rovira C, Davis BG
Nat Chem Biol 13 874-881 (2017)
PMID: 28604696

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149650 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 489 amino acids
Theoretical weight: 56.79 KDa
Source organism: Saccharolobus solfataricus P2
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P22498 (Residues: 1-489; Coverage: 100%)
Gene names: SSO3019, lacS
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand PE8 1 x PE8
Ligand ACT 15 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 92.68Å b: 129.06Å c: 191.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.203
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

3 review citations

Chemoenzymatic Methods for the Synthesis of Glycoproteins.
Li et al. (2018)
2 more

2 mentions without citation

The Bombyx mori karyotype and the assignment of linkage groups.
Yoshido et al. (2005)
1 more