› 20gs

X-ray diffraction
2.45Å resolution

GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE

Released:
DOI: 10.2210/pdb20gs/pdb
PDB entry 20gs coloured by chain, front view.
PDB entry 20gs coloured by chain, side view.
PDB entry 20gs 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: 209 amino acids
Theoretical weight: 23.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MES 2 x MES
Ligand CBD 2 x CBD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 78.176Å b: 90.69Å c: 68.755Å
α: 90° β: 97.73° γ: 90°
R-values:
R R work R free
0.229 0.229 0.28
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

2 mentions without citation

Comprehensive analysis of the catalytic and structural properties of a mu-class glutathione s-transferase from Fasciola gigantica.
Kalita et al. (2017)
1 more