› 3lfl

X-ray diffraction
2.1Å resolution

Crystal Structure of human Glutathione Transferase Omega 1, delta 155

Released:
DOI: 10.2210/pdb3lfl/pdb
PDB entry 3lfl coloured by chain, front view.
PDB entry 3lfl coloured by chain, side view.
PDB entry 3lfl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1.
Zhou H, Brock J, Casarotto MG, Oakley AJ, Board PG
J Biol Chem 286 4271-9 (2011)
PMID: 21106529

Function and Biology Details

Reactions catalysed: 
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H(2)O
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
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-160265 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase omega-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 240 amino acids
Theoretical weight: 27.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P78417 (Residues: 1-241; Coverage: 100%)
Gene names: GSTO1, GSTTLP28
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 3 x GSH
1 bound ligand:
Ligand DTT 3 x DTT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 73.009Å b: 201.942Å c: 53.387Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.255
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Glutathione transferases, regulators of cellular metabolism and physiology.
Board et al. (2013)
4 more

4 mentions without citation

Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1.
Zhou et al. (2011)
3 more