PDBe 3gst

X-ray diffraction
1.9Å resolution

STRUCTURE OF THE XENOBIOTIC SUBSTRATE BINDING SITE OF A GLUTATHIONE S-TRANSFERASE AS REVEALED BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PRODUCT COMPLEXES WITH THE DIASTEREOMERS OF 9-(S-GLUTATHIONYL)-10-HYDROXY-9, 10-DIHYDROPHENANTHRENE

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 25.82 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
  • Canonical: P04905 (Residues: 2-218; Coverage: 100%)
Gene name: Gstm1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 88.24Å b: 69.44Å c: 81.28Å
α: 90° β: 106.01° γ: 90°
R-values:
R R work R free
0.159 not available not available
Expression system: Not provided