› 3ljr

X-ray diffraction
3.3Å resolution

GLUTATHIONE TRANSFERASE (THETA CLASS) FROM HUMAN IN COMPLEX WITH THE GLUTATHIONE CONJUGATE OF 1-MENAPHTHYL SULFATE

Released:
DOI: 10.2210/pdb3ljr/pdb
PDB entry 3ljr coloured by chain, front view.
PDB entry 3ljr coloured by chain, side view.
PDB entry 3ljr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
Rossjohn J, McKinstry WJ, Oakley AJ, Verger D, Flanagan J, Chelvanayagam G, Tan KL, Board PG, Parker MW
Structure 6 309-22 (1998)
PMID: 9551553

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase theta-2B Chains: A, B
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 27.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG30 (Residues: 1-244; Coverage: 100%)
Gene names: GSTT2, GSTT2B
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GGC 2 x GGC
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P3121
Unit cell:
a: 94.065Å b: 94.065Å c: 120.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.335
Expression system: Escherichia coli

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Citations

15 review citations

Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
Sheehan et al. (2001)
14 more

3 mentions without citation

X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
Fritz-Wolf et al. (2003)
2 more