› 2c3q

X-ray diffraction
1.85Å resolution

Human glutathione-S-transferase T1-1 W234R mutant, complex with S- hexylglutathione

Released:
DOI: 10.2210/pdb2c3q/pdb
PDB entry 2c3q coloured by chain, front view.
PDB entry 2c3q coloured by chain, side view.
PDB entry 2c3q 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


Cofactor: Ligand GTX 4 x GTX
1 bound ligand:
Ligand IOD 31 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 54.499Å b: 109.683Å c: 171.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.223 0.252
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

7 mentions without citation

The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.
Griswold et al. (2006)
6 more