› 2x16

X-ray diffraction
2.13Å resolution

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

Released:
DOI: 10.2210/pdb2x16/pdb
PDB entry 2x16 coloured by chain, front view.
PDB entry 2x16 coloured by chain, side view.
PDB entry 2x16 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 45.49Å b: 85.3Å c: 55.88Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.184 0.18 0.261
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

1 mention without citation

Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.
Krause et al. (2016)