1ags

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:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (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: Glutathione S-transferase, N-terminal domain

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