5ddl

X-ray diffraction
1.98Å resolution

Crystal Structure of WT Human Glutathione Transferase Pi soaked with a metalloid then back-soaked with glutathione

Released:
Source organism: Homo sapiens
Entry authors: Parker LJ, Parker MW, Morton CJ

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: 210 amino acids
Theoretical weight: 23.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 1-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 5AU 2 x 5AU

Cofactor: Ligand GSH 2 x GSH
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 77.665Å b: 89.795Å c: 68.854Å
α: 90° β: 98.08° γ: 90°
R-values:
R R work R free
0.14 0.138 0.178
Expression system: Escherichia coli