› 1gum

X-ray diffraction
3Å resolution

HUMAN GLUTATHIONE TRANSFERASE A4-4 WITHOUT LIGANDS

Released:
DOI: 10.2210/pdb1gum/pdb
PDB entry 1gum coloured by chain, front view.
PDB entry 1gum coloured by chain, side view.
PDB entry 1gum coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products.
Bruns CM, Hubatsch I, Ridderström M, Mannervik B, Tainer JA
J Mol Biol 288 427-39 (1999)
PMID: 10329152

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-127354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A4 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 222 amino acids
Theoretical weight: 25.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15217 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA4
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21212
Unit cell:
a: 155.3Å b: 156.1Å c: 101.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.253 0.27
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress.
Butterfield et al. (2002)
11 more

5 mentions without citation

Interactions of glutathione transferases with 4-hydroxynonenal.
Balogh et al. (2011)
4 more