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X-ray diffraction
2.3Å resolution

Leishmania TDR1 - a unique trimeric glutathione transferase

Released:
DOI: 10.2210/pdb4ags/pdb
PDB entry 4ags coloured by chain, front view.
PDB entry 4ags coloured by chain, side view.
PDB entry 4ags coloured by chain, top view.
Source organism: Leishmania infantum
Primary publication:
Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation.
Fyfe PK, Westrop GD, Silva AM, Coombs GH, Hunter WN
Proc Natl Acad Sci U S A 109 11693-8 (2012)
PMID: 22753509

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol-dependent reductase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 471 amino acids
Theoretical weight: 53.2 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli B
UniProt:
  • Canonical: A4I8P2 (Residues: 1-450; Coverage: 100%)
Gene names: LINJ_33_0260, TDR1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GSH 6 x GSH
Ligand EDO 15 x EDO
1 modified residue:
Ligand MSE 51 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 197.477Å b: 58.396Å c: 160.385Å
α: 90° β: 111.81° γ: 90°
R-values:
R R work R free
0.152 0.149 0.208
Expression system: Escherichia coli B

Quick links

Citations

6 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
5 more

6 mentions without citation

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