› 1q1q

X-ray diffraction
2.91Å resolution

Crystal structure of human pregnenolone sulfotransferase (SULT2B1a) in the presence of PAP

Released:
DOI: 10.2210/pdb1q1q/pdb
PDB entry 1q1q coloured by chain, front view.
PDB entry 1q1q coloured by chain, side view.
PDB entry 1q1q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms.
Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC
J Biol Chem 278 44593-9 (2003)
PMID: 12923182

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126149 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 2B1 Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 39.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00204 (Residues: 24-365; Coverage: 94%)
Gene names: HSST2, SULT2B1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand NA 1 x NA
Ligand A3P 1 x A3P
Ligand NHE 2 x NHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P41212
Unit cell:
a: 75.244Å b: 75.244Å c: 252.246Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.249 0.269
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

13 mentions without citation

The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases.
Rižner TL. (2016)
12 more