› 1eog

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE

Released:
DOI: 10.2210/pdb1eog/pdb
PDB entry 1eog coloured by chain, front view.
PDB entry 1eog coloured by chain, side view.
PDB entry 1eog 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
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 3-210; Coverage: 99%)
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
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 79.87Å b: 91.01Å c: 69.07Å
α: 90° β: 98.78° γ: 90°
R-values:
R R work R free
0.204 0.204 0.238
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

5 mentions without citation

Murein and pseudomurein cell wall binding domains of bacteria and archaea--a comparative view.
Visweswaran et al. (2011)
4 more