› 1aqw

X-ray diffraction
1.8Å resolution

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE

Released:
DOI: 10.2210/pdb1aqw/pdb
PDB entry 1aqw coloured by chain, front view.
PDB entry 1aqw coloured by chain, side view.
PDB entry 1aqw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.
Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W
Structure 5 1287-95 (1997)
PMID: 9351803

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-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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 4 x GSH
1 bound ligand:
Ligand MES 4 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 90.29Å b: 74.67Å c: 69.5Å
α: 90° β: 90.07° γ: 90°
R-values:
R R work R free
0.206 0.206 0.261
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
7 more

8 mentions without citation

Copper Sources for Sod1 Activation.
Boyd et al. (2020)
7 more