› 1k3o

X-ray diffraction
1.8Å resolution

Crystal Structure Analysis of apo Glutathione S-Transferase

Released:
DOI: 10.2210/pdb1k3o/pdb
PDB entry 1k3o coloured by chain, front view.
PDB entry 1k3o coloured by chain, side view.
PDB entry 1k3o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site.
Le Trong I, Stenkamp RE, Ibarra C, Atkins WM, Adman ET
Proteins 48 618-27 (2002)
PMID: 12211029

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-140083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 25.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08263 (Residues: 2-222; Coverage: 100%)
Gene name: GSTA1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 102.383Å b: 96.007Å c: 52.889Å
α: 90° β: 92.94° γ: 90°
R-values:
R R work R free
0.248 0.246 0.336
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

3 mentions without citation

Enzymatic detoxication, conformational selection, and the role of molten globule active sites.
Honaker et al. (2013)
2 more