› 3bgi

X-ray diffraction
1.8Å resolution

Thiopurine S-Methyltransferase

Released:
DOI: 10.2210/pdb3bgi/pdb
PDB entry 3bgi coloured by chain, front view.
PDB entry 3bgi coloured by chain, side view.
PDB entry 3bgi coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis of substrate recognition in thiopurine s-methyltransferase.
Peng Y, Feng Q, Wilk D, Adjei AA, Salavaggione OE, Weinshilboum RM, Yee VC
Biochemistry 47 6216-25 (2008)
PMID: 18484748

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiopurine S-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 29.8 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O55060 (Residues: 1-240; Coverage: 100%)
Gene name: Tpmt
Sequence domains: Thiopurine S-methyltransferase (TPMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 62.908Å b: 65.513Å c: 72.897Å
α: 90° β: 115.29° γ: 90°
R-values:
R R work R free
0.189 0.187 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
1 more

1 mention without citation

Structural basis of substrate recognition in thiopurine s-methyltransferase.
Peng et al. (2008)