› 1pmt

X-ray diffraction
2.5Å resolution

GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS

Released:
DOI: 10.2210/pdb1pmt/pdb
PDB entry 1pmt coloured by chain, front view.
PDB entry 1pmt coloured by chain, side view.
PDB entry 1pmt coloured by chain, top view.
Source organism: Proteus mirabilis
Primary publication:
A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications.
Rossjohn J, Polekhina G, Feil SC, Allocati N, Masulli M, Di Illio C, Parker MW
Structure 6 721-34 (1998)
PMID: 9655824

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase GST-6.0 Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 22.88 KDa
Source organism: Proteus mirabilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P15214 (Residues: 1-203; Coverage: 100%)
Gene name: gstB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P4122
Unit cell:
a: 57.2Å b: 57.2Å c: 129.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.301
Expression system: Escherichia coli

Quick links

Citations

11 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)
10 more

8 mentions without citation

The still mysterious roles of cysteine-containing glutathione transferases in plants.
Lallement et al. (2014)
7 more