› 18gs

X-ray diffraction
1.9Å resolution

GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE

Released:
DOI: 10.2210/pdb18gs/pdb
PDB entry 18gs coloured by chain, front view.
PDB entry 18gs coloured by chain, side view.
PDB entry 18gs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site).
Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW
J Mol Biol 291 913-26 (1999)
PMID: 10452896

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-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 1-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GDN 2 x GDN
1 bound ligand:
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 78.502Å b: 89.635Å c: 68.907Å
α: 90° β: 97.54° γ: 90°
R-values:
R R work R free
0.181 0.181 0.238
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

10 mentions without citation

Glutathione transferases of Phanerochaete chrysosporium: S-glutathionyl-p-hydroquinone reductase belongs to a new structural class.
Meux et al. (2011)
9 more