› 2f51

X-ray diffraction
1.9Å resolution

Structure of Trichomonas vaginalis thioredoxin

Released:
DOI: 10.2210/pdb2f51/pdb
PDB entry 2f51 coloured by chain, front view.
PDB entry 2f51 coloured by chain, side view.
PDB entry 2f51 coloured by chain, top view.
Source organism: Trichomonas vaginalis
Primary publication:
High-resolution structure of recombinant Trichomonas vaginalis thioredoxin.
Iulek J, Alphey MS, Westrop GD, Coombs GH, Hunter WN
Acta Crystallogr D Biol Crystallogr 62 216-20 (2006)
PMID: 16421453

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184759 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.11 KDa
Source organism: Trichomonas vaginalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IEV4 (Residues: 1-112; Coverage: 100%)
Gene name: trx
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 33.882Å b: 33.923Å c: 50.497Å
α: 106.2° β: 109.02° γ: 91.68°
R-values:
R R work R free
0.147 0.145 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Metabolomic profiling and stable isotope labelling of Trichomonas vaginalis and Tritrichomonas foetus reveal major differences in amino acid metabolism including the production of 2-hydroxyisocaproic acid, cystathionine and S-methylcysteine.
Westrop et al. (2017)

1 mention without citation

Disulfide conformation and design at helix N-termini.
Indu et al. (2010)