› 2c3t

X-ray diffraction
2.4Å resolution

Human glutathione-S-transferase T1-1, W234R mutant, apo form

Released:
DOI: 10.2210/pdb2c3t/pdb
PDB entry 2c3t coloured by chain, front view.
PDB entry 2c3t coloured by chain, side view.
PDB entry 2c3t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant.
Tars K, Larsson AK, Shokeer A, Olin B, Mannervik B, Kleywegt GJ
J Mol Biol 355 96-105 (2006)
PMID: 16298388

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151793 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase theta-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 247 amino acids
Theoretical weight: 28.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30711 (Residues: 1-240; Coverage: 100%)
Gene name: GSTT1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 164.524Å b: 111.822Å c: 55.924Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.213 0.267
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Glutathione transferases, regulators of cellular metabolism and physiology.
Board et al. (2013)
3 more

1 mention without citation

Glutathione-binding site of a bombyx mori theta-class glutathione transferase.
Hossain et al. (2014)