› 1m99

X-ray diffraction
2.3Å resolution

Crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum complexed with glutathione sulfonic acid

Released:
DOI: 10.2210/pdb1m99/pdb
PDB entry 1m99 coloured by chain, front view.
PDB entry 1m99 coloured by chain, side view.
PDB entry 1m99 coloured by chain, top view.
Source organism: Schistosoma japonicum
Primary publication:
Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum.
Cardoso RM, Daniels DS, Bruns CM, Tainer JA
Proteins 51 137-46 (2003)
PMID: 12596270

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-530668 (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: 25.53 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 GTS 1 x GTS
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6322
Unit cell:
a: 115.07Å b: 115.07Å c: 78.28Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.261
Expression system: Escherichia coli

Quick links

Citations

23 citation in other articles

Nucleophilic catalysis of acylhydrazone equilibration for protein-directed dynamic covalent chemistry.
Bhat et al. (2010)
22 more

5 mentions without citation

The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism.
Quintana-Gallardo et al. (2019)
4 more