› 3gur

X-ray diffraction
2.5Å resolution

Crystal Structure of mu class glutathione S-transferase (GSTM2-2) in complex with glutathione and 6-(7-Nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol (NBDHEX)

Released:
DOI: 10.2210/pdb3gur/pdb
PDB entry 3gur coloured by chain, front view.
PDB entry 3gur coloured by chain, side view.
PDB entry 3gur coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.
Federici L, Lo Sterzo C, Pezzola S, Di Matteo A, Scaloni F, Federici G, Caccuri AM
Cancer Res 69 8025-34 (2009)
PMID: 19808963

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151172 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 217 amino acids
Theoretical weight: 25.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28161 (Residues: 2-218; Coverage: 100%)
Gene names: GST4, GSTM2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BYG 2 x BYG

Cofactor: Ligand GSH 2 x GSH
1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 56.75Å b: 78.016Å c: 219.362Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.213 0.273
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death.
Laborde E. (2010)
10 more

4 mentions without citation

Proteomic and functional analyses reveal pleiotropic action of the anti-tumoral compound NBDHEX in Giardia duodenalis.
Camerini et al. (2017)
3 more