› 4jvn

X-ray diffraction
2.05Å resolution

Crystal structure of human estrogen sulfotransferase (SULT1E1) in complex with inactive cofactor PAP and metabolite of brominated flame retardant 3OH BDE47 (3-hydroxyl bromodiphenyl ether)

Released:
DOI: 10.2210/pdb4jvn/pdb
PDB entry 4jvn coloured by chain, front view.
PDB entry 4jvn coloured by chain, side view.
PDB entry 4jvn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mimicking of estradiol binding by flame retardants and their metabolites: a crystallographic analysis.
Gosavi RA, Knudsen GA, Birnbaum LS, Pedersen LC
Environ Health Perspect 121 1194-9 (2013)
PMID: 23959441

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 1E1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 35.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

4 bound ligands:
Ligand YUG 2 x YUG
Ligand A3P 2 x A3P
Ligand NA 2 x NA
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 62.676Å b: 96.989Å c: 61.389Å
α: 90° β: 92.44° γ: 90°
R-values:
R R work R free
0.187 0.185 0.236
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The Regulation of Steroid Action by Sulfation and Desulfation.
Mueller et al. (2015)
7 more

5 mentions without citation

Estrogen Sulfotransferase (SULT1E1): Its Molecular Regulation, Polymorphisms, and Clinical Perspectives.
Yi et al. (2021)
4 more