X-ray diffraction
1.58Å resolution

Crystal structure of thiopurine S-methyltransferase.


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Thiopurine S-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 26.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P51580 (Residues: 14-245; Coverage: 95%)
Gene name: TPMT
Sequence domains: Thiopurine S-methyltransferase (TPMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P42212
Unit cell:
a: 85.486Å b: 85.486Å c: 69.362Å
α: 90° β: 90° γ: 90°
R R work R free
0.214 0.213 0.249
Expression system: Escherichia coli