› 1ls6

X-ray diffraction
1.9Å resolution

Human SULT1A1 complexed with PAP and p-Nitrophenol

Released:
DOI: 10.2210/pdb1ls6/pdb
PDB entry 1ls6 coloured by chain, front view.
PDB entry 1ls6 coloured by chain, side view.
PDB entry 1ls6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition.
Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, Liyou NE, McManus ME, Martin JL
J Biol Chem 278 7655-62 (2003)
PMID: 12471039

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156147 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 1A1 Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand A3P 1 x A3P
Ligand NPO 2 x NPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 72.8Å b: 124.01Å c: 44.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.181 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

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

21 mentions without citation

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