› 2x1r

X-ray diffraction
1.98Å resolution

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

Released:
DOI: 10.2210/pdb2x1r/pdb
PDB entry 2x1r coloured by chain, front view.
PDB entry 2x1r coloured by chain, side view.
PDB entry 2x1r coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase.
Salin M, Kapetaniou EG, Vaismaa M, Lajunen M, Casteleijn MG, Neubauer P, Salmon L, Wierenga RK
Acta Crystallogr D Biol Crystallogr 66 934-44 (2010)
PMID: 20693693

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138175 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 25.66 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 2-250; Coverage: 95%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand X1R 2 x X1R
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 45.94Å b: 86.92Å c: 56.28Å
α: 90° β: 98.58° γ: 90°
R-values:
R R work R free
0.164 0.161 0.226
Expression system: Escherichia coli BL21

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Citations

1 review citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 other articles