› 1ml6

X-ray diffraction
1.9Å resolution

Crystal Structure of mGSTA2-2 in Complex with the Glutathione Conjugate of Benzo[a]pyrene-7(R),8(S)-Diol-9(S),10(R)-Epoxide

Released:
DOI: 10.2210/pdb1ml6/pdb
PDB entry 1ml6 coloured by chain, front view.
PDB entry 1ml6 coloured by chain, side view.
PDB entry 1ml6 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide.
Gu Y, Xiao B, Wargo HL, Bucher MH, Singh SV, Ji X
Biochemistry 42 917-21 (2003)
PMID: 12549910

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-145416 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 25.46 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10648 (Residues: 2-222; Coverage: 100%)
Gene name: Gsta2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GBX 2 x GBX
1 bound ligand:
Ligand IPA 2 x IPA
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: C2
Unit cell:
a: 99.067Å b: 93.903Å c: 52.6Å
α: 90° β: 92.28° γ: 90°
R-values:
R R work R free
0.2 0.2 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Glutathione transferases: a structural perspective.
Oakley A. (2011)
1 other article

2 mentions without citation

Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Atkinson et al. (2009)
1 more