PDBe 1px6

X-ray diffraction
2.1Å resolution

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

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: 23.25 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


Cofactor: Ligand GSH 2 x GSH
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 69.21Å b: 78.76Å c: 89.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.19 0.235
Expression system: Escherichia coli