› 1q22

X-ray diffraction
2.5Å resolution

Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP

Released:
DOI: 10.2210/pdb1q22/pdb
PDB entry 1q22 coloured by chain, front view.
PDB entry 1q22 coloured by chain, side view.
PDB entry 1q22 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:
  • not assigned
Cellular component:
  • not assigned
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: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00204 (Residues: 19-312; Coverage: 81%)
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 AND 1 x AND
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P41212
Unit cell:
a: 75.859Å b: 75.859Å c: 253.807Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.221 0.252
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

131 mentions without citation

The SET-domain protein superfamily: protein lysine methyltransferases.
Dillon et al. (2005)
130 more