› 2rm6

Solution NMR

Glutathione peroxidase-type tryparedoxin peroxidase, reduced form

Released:
DOI: 10.2210/pdb2rm6/pdb
PDB entry 2rm6 coloured by chain, ensemble of 20 models, front view.
PDB entry 2rm6 coloured by chain, ensemble of 20 models, side view.
PDB entry 2rm6 coloured by chain, ensemble of 20 models, top view.
Source organism: Trypanosoma brucei
Primary publication:
Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.
Melchers J, Diechtierow M, Fehér K, Sinning I, Tews I, Krauth-Siegel RL, Muhle-Goll C
J Biol Chem 283 30401-11 (2008)
PMID: 18684708

Function and Biology Details

Reaction catalysed: 
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183112 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione peroxidase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 18.6 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q869A5 (Residues: 13-176; Coverage: 93%)
Gene name: gpx3
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase.
Melchers et al. (2008)