› 2j24

X-ray diffraction
2.1Å resolution

The functional role of the conserved active site proline of triosephosphate isomerase

Released:
DOI: 10.2210/pdb2j24/pdb
PDB entry 2j24 coloured by chain, front view.
PDB entry 2j24 coloured by chain, side view.
PDB entry 2j24 coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Functional role of the conserved active site proline of triosephosphate isomerase.
Casteleijn MG, Alahuhta M, Groebel K, El-Sayed I, Augustyns K, Lambeir AM, Neubauer P, Wierenga RK
Biochemistry 45 15483-94 (2006)
PMID: 17176070

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.84 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
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: ENRAF-NONIUS FR591
Spacegroup: P1
Unit cell:
a: 37.5Å b: 43.72Å c: 71.27Å
α: 80.49° β: 79.61° γ: 64.66°
R-values:
R R work R free
0.153 0.149 0.23
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
4 more

3 mentions without 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)
2 more