› 6gst

X-ray diffraction
2.2Å resolution

FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE

Released:
DOI: 10.2210/pdb6gst/pdb
PDB entry 6gst coloured by chain, front view.
PDB entry 6gst coloured by chain, side view.
PDB entry 6gst coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase.
Xiao G, Liu S, Ji X, Johnson WW, Chen J, Parsons JF, Stevens WJ, Gilliland GL, Armstrong RN
Biochemistry 35 4753-65 (1996)
PMID: 8664265

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-138255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 25.82 KDa
Source organism: Rattus rattus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04905 (Residues: 2-218; Coverage: 100%)
Gene name: Gstm1
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 88.24Å b: 69.44Å c: 81.28Å
α: 90° β: 106.01° γ: 90°
R-values:
R R work R free
0.149 0.149 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
Sheehan et al. (2001)
7 more

8 mentions without citation

Comparison of protein acetyltransferase action of CRTAase with the prototypes of HAT.
Ponnan et al. (2014)
7 more