› 1eoh

X-ray diffraction
2.5Å resolution

GLUTATHIONE TRANSFERASE P1-1

Released:
DOI: 10.2210/pdb1eoh/pdb
PDB entry 1eoh coloured by chain, front view.
PDB entry 1eoh coloured by chain, side view.
PDB entry 1eoh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of thermolabile mutants of human glutathione transferase P1-1.
Rossjohn J, McKinstry WJ, Oakley AJ, Parker MW, Stenberg G, Mannervik B, Dragani B, Cocco R, Aceto A
J Mol Biol 302 295-302 (2000)
PMID: 10970734

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, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 209 amino acids
Theoretical weight: 23.2 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 82.97Å b: 84.02Å c: 236.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.231 0.286
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation.
Gallo et al. (2005)
10 more

1 mention without citation

Cytokine/chemokine secretion and proteomic identification of upregulated annexin A1 from peripheral blood mononuclear cells cocultured with the liver fluke Opisthorchis viverrini.
Hongsrichan et al. (2014)