› 1pl2

X-ray diffraction
1.8Å resolution

Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione

Released:
DOI: 10.2210/pdb1pl2/pdb
PDB entry 1pl2 coloured by chain, front view.
PDB entry 1pl2 coloured by chain, side view.
PDB entry 1pl2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.
Grahn E, Novotny M, Jakobsson E, Gustafsson A, Grehn L, Olin B, Madsen D, Wahlberg M, Mannervik B, Kleywegt GJ
Acta Crystallogr D Biol Crystallogr 62 197-207 (2006)
PMID: 16421451

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: 222 amino acids
Theoretical weight: 25.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08263 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand ABY 2 x ABY
1 bound ligand:
Ligand CL 2 x CL
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: C2
Unit cell:
a: 99.233Å b: 90.695Å c: 51.158Å
α: 90° β: 93.39° γ: 90°
R-values:
R R work R free
0.165 0.161 0.2
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

In-silico prediction of drug targets, biological activities, signal pathways and regulating networks of dioscin based on bioinformatics.
Yin et al. (2015)