› 1u87

X-ray diffraction
3.5Å resolution

Crystal Structure Of The 26 Kda Glutathione S-Transferase Y7F mutant From Schistosoma Japonicum Complexed With Glutathione

Released:
DOI: 10.2210/pdb1u87/pdb
PDB entry 1u87 coloured by chain, front view.
PDB entry 1u87 coloured by chain, side view.
PDB entry 1u87 coloured by chain, top view.
Source organism: Schistosoma japonicum
Primary publication:
Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.
Andújar-Sánchez M, Smith AW, Clemente-Jimenez JM, Rodriguez-Vico F, Las Heras-Vazquez FJ, Jara-Pérez V, Cámara-Artigas A
Biochemistry 44 1174-83 (2005)
PMID: 15667211

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase class-mu 26 kDa isozyme Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 25.52 KDa
Source organism: Schistosoma japonicum
Expression system: Escherichia coli
UniProt:
  • Canonical: P08515 (Residues: 1-218; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200HB
Spacegroup: P6322
Unit cell:
a: 123.05Å b: 123.05Å c: 72.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.199 0.271
Expression system: Escherichia coli

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Citations

1 review citation

Survey of the year 2005: literature on applications of isothermal titration calorimetry.
Ababou et al. (2007)
10 other articles

2 mentions without citation

Hybrid Steered Molecular Dynamics Approach to Computing Absolute Binding Free Energy of Ligand-Protein Complexes: A Brute Force Approach That Is Fast and Accurate.
Chen LY. (2015)
1 more