› 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:
DOI: 10.2210/pdb3gst/pdb
PDB entry 3gst coloured by chain, front view.
PDB entry 3gst coloured by chain, side view.
PDB entry 3gst coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
Structure and function 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.
Ji X, Johnson WW, Sesay MA, Dickert L, Prasad SM, Ammon HL, Armstrong RN, Gilliland GL
Biochemistry 33 1043-52 (1994)
PMID: 8110735

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-138255 (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


Cofactor: Ligand GPR 2 x GPR
1 bound ligand:
Ligand SO4 7 x SO4
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

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Citations

12 review citations

The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.
Hayes et al. (1995)
11 more

1 mention without citation

β3 integrin interacts directly with GluA2 AMPA receptor subunit and regulates AMPA receptor expression in hippocampal neurons.
Pozo et al. (2012)