› 2cfu

X-ray diffraction
1.9Å resolution

Crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, in complex with 1-decane-sulfonic-acid.

Released:
DOI: 10.2210/pdb2cfu/pdb
PDB entry 2cfu coloured by chain, front view.
PDB entry 2cfu coloured by chain, side view.
PDB entry 2cfu coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases.
Hagelueken G, Adams TM, Wiehlmann L, Widow U, Kolmar H, Tümmler B, Heinz DW, Schubert WD
Proc Natl Acad Sci U S A 103 7631-6 (2006)
PMID: 16684886

Function and Biology Details

Reaction catalysed: 
A primary alkyl sulfate ester + H(2)O = an alcohol + sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191425 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Linear primary-alkylsulfatase Chain: A
Molecule details ›
Chain: A
Length: 658 amino acids
Theoretical weight: 72.67 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I5I9 (Residues: 1-658; Coverage: 100%)
Gene names: PA0740, sdsA1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand 1DB 1 x 1DB
Ligand PEG 8 x PEG
Ligand IPA 1 x IPA
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6522
Unit cell:
a: 86.057Å b: 86.057Å c: 364.413Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.171 0.217
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily.
Bebrone C. (2007)
9 more

6 mentions without citation

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
5 more