› 1z28

X-ray diffraction
2.3Å resolution

Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

Released:
DOI: 10.2210/pdb1z28/pdb
PDB entry 1z28 coloured by chain, front view.
PDB entry 1z28 coloured by chain, side view.
PDB entry 1z28 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2.
Lu J, Li H, Zhang J, Li M, Liu MY, An X, Liu MC, Chang W
Biochem Biophys Res Commun 396 429-34 (2010)
PMID: 20417180

Function and Biology Details

Reaction catalysed: 
3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 1A1 Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P50225 (Residues: 1-295; Coverage: 100%)
Gene names: OK/SW-cl.88, STP, STP1, SULT1A1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand A3P 1 x A3P
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 72.24Å b: 122.53Å c: 43.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.193 0.231
Expression system: Escherichia coli BL21

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Citations

4 review citations

Substrate inhibition kinetics in drug metabolism reactions.
Wu B. (2011)
3 more

6 mentions without citation

The structural biology of oestrogen metabolism.
Thomas et al. (2013)
5 more