› 1hdh

X-ray diffraction
1.3Å resolution

Function and Biology Details

Reaction catalysed: 
An aryl sulfate + H(2)O = a phenol + sulfate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylsulfatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 536 amino acids
Theoretical weight: 60.02 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P51691 (Residues: 1-536; Coverage: 100%)
Gene names: PA0183, atsA
Sequence domains: Sulfatase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand SO4 8 x SO4
1 modified residue:
Ligand DDZ 2 x DDZ

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 188.92Å b: 67.29Å c: 89.7Å
α: 90° β: 94.2° γ: 90°
R-values:
R R work R free
0.2 not available 0.228
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.
Hanson et al. (2004)
14 more

26 mentions without citation

Heparin-degrading sulfatases in hepatocellular carcinoma: roles in pathogenesis and therapy targets.
Lai et al. (2008)
25 more