› 1lbk

X-ray diffraction
1.86Å resolution

Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

Released:
DOI: 10.2210/pdb1lbk/pdb
PDB entry 1lbk coloured by chain, front view.
PDB entry 1lbk coloured by chain, side view.
PDB entry 1lbk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Engineering a new C-terminal tail in the H-site of human glutathione transferase P1-1: structural and functional consequences.
Micaloni C, Kong GK, Mazzetti AP, Nuccetelli M, Antonini G, Stella L, McKinstry WJ, Polekhina G, Rossjohn J, Federici G, Ricci G, Parker MW, Lo Bello M
J Mol Biol 325 111-22 (2003)
PMID: 12473455

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-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-205; Coverage: 97%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:
Ligand MES 2 x MES
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 68.3Å b: 79.3Å c: 89.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.224
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases.
Axarli et al. (2009)
5 more

1 mention without citation

Visualization of the hybrid state of tRNA binding promoted by spontaneous ratcheting of the ribosome.
Agirrezabala et al. (2008)