PDBe 1px7

X-ray diffraction
2.03Å resolution

A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate

Released:
Source organism: Homo sapiens
Entry authors: Kong GK-W, Polekhina G, McKinstry WJ, Parker MW, Dragani B, Aceto A, Paludi D, Principe DR, Mannervik B, Stenberg G

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (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: 23.26 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


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 77.75Å b: 89.33Å c: 68.79Å
α: 90° β: 97.88° γ: 90°
R-values:
R R work R free
0.2 0.177 0.218
Expression system: Escherichia coli