› 1g3m

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL

Released:
DOI: 10.2210/pdb1g3m/pdb
PDB entry 1g3m coloured by chain, front view.
PDB entry 1g3m coloured by chain, side view.
PDB entry 1g3m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase.
Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M
Environ Health Perspect 111 884-8 (2003)
PMID: 12782487

Function and Biology Details

Reaction catalysed: 
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156072 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 1E1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 35.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49888 (Residues: 1-294; Coverage: 100%)
Gene names: STE, SULT1E1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand A3P 2 x A3P
Ligand PCQ 2 x PCQ
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 62.687Å b: 96.894Å c: 61.724Å
α: 90° β: 92.58° γ: 90°
R-values:
R R work R free
0.193 0.193 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Human sulfotransferases and their role in chemical metabolism.
Gamage et al. (2006)
2 more

18 mentions without citation

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