› 1gxf

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE IN COMPLEX WITH THE INHIBITOR QUINACRINE MUSTARD

Released:
DOI: 10.2210/pdb1gxf/pdb
PDB entry 1gxf coloured by chain, front view.
PDB entry 1gxf coloured by chain, side view.
PDB entry 1gxf coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design.
Saravanamuthu A, Vickers TJ, Bond CS, Peterson MR, Hunter WN, Fairlamb AH
J Biol Chem 279 29493-500 (2004)
PMID: 15102853

Function and Biology Details

Reaction catalysed: 
Trypanothione + NADP(+) = trypanothione disulfide + NADPH
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-151248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypanothione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 492 amino acids
Theoretical weight: 53.93 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: P28593 (Residues: 1-492; Coverage: 100%)
Gene name: TPR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand MAE 1 x MAE
Ligand QUM 4 x QUM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P43
Unit cell:
a: 93.1Å b: 93.1Å c: 156.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.25
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Opportunities and challenges in antiparasitic drug discovery.
Pink et al. (2005)
7 more

7 mentions without citation

Thioredoxin reductase and its inhibitors.
Saccoccia et al. (2014)
6 more