› 2gtu

X-ray diffraction
2.55Å resolution

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb2gtu/pdb
PDB entry 2gtu coloured by chain, front view.
PDB entry 2gtu coloured by chain, side view.
PDB entry 2gtu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.
Patskovsky YV, Patskovska LN, Listowsky I
J Biol Chem 275 3296-304 (2000)
PMID: 10652317

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-151172 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 25.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28161 (Residues: 2-218; Coverage: 100%)
Gene names: GST4, GSTM2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 53.909Å b: 81.479Å c: 55.621Å
α: 90° β: 109.26° γ: 90°
R-values:
R R work R free
0.203 0.203 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Glutathione transferases.
Hayes et al. (2005)
1 more

1 mention without citation

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution.
Norrgård et al. (2006)