› 4p06

X-ray diffraction
2.1Å resolution

Bacterial arylsulfate sulfotransferase (ASST) H436N mutant with 4-methylumbelliferyl sulfate (MUS) in the active site

Released:
DOI: 10.2210/pdb4p06/pdb
PDB entry 4p06 coloured by chain, front view.
PDB entry 4p06 coloured by chain, side view.
PDB entry 4p06 coloured by chain, top view.
Source organism: Escherichia coli CFT073
Primary publication:
Structural and mechanistic insights into the PAPS-independent sulfotransfer catalyzed by bacterial aryl sulfotransferase and the role of the DsbL/Dsbl system in its folding.
Malojčić G, Owen RL, Glockshuber R
Biochemistry 53 1870-7 (2014)
PMID: 24601529

Function and Biology Details

Reaction catalysed: 
An aryl sulfate + a phenol = a phenol + an aryl sulfate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-101139 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylsulfate sulfotransferase AssT Chains: A, B
Molecule details ›
Chains: A, B
Length: 571 amino acids
Theoretical weight: 63.82 KDa
Source organism: Escherichia coli CFT073
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0D6H805 (Residues: 28-598; Coverage: 100%)
Gene names: A5U30_002410, BR158_000010, C2121_000443, D3C88_14135, EWK56_03515, F7F11_17305, FPI65_18875, GFY48_06085, HI055_000207, NCTC10767_01803, NCTC9001_05799, NCTC9081_01241, assT
Sequence domains:
Structure domains: Arylsulphate sulphotransferase monomer, N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand MUX 2 x MUX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3212
Unit cell:
a: 181.533Å b: 181.533Å c: 100.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.163 0.185
Expression system: Escherichia coli

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Citations

3 review citations

Sulfation pathways from red to green.
Günal et al. (2019)
2 more