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X-ray diffraction
2.5Å resolution

A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL

Released:
DOI: 10.2210/pdb1ags/pdb
PDB entry 1ags coloured by chain, front view.
PDB entry 1ags coloured by chain, side view.
PDB entry 1ags coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.
Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC
Proteins 20 259-63 (1994)
PMID: 7892174

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-140590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 25.69 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: P09210 (Residues: 2-222; Coverage: 100%)
Gene names: GST2, GSTA2
Sequence domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 49.5Å b: 92.9Å c: 115.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.31 0.31 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Modeling the active sites of cytochrome P450s and glutathione S-transferases, two of the most important biotransformation enzymes.
De Groot et al. (1997)
1 more