› 1iig

X-ray diffraction
2.6Å resolution

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE

Released:
DOI: 10.2210/pdb1iig/pdb
PDB entry 1iig coloured by chain, front view.
PDB entry 1iig coloured by chain, side view.
PDB entry 1iig coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG
Proteins 10 50-69 (1991)
PMID: 2062828

Function and Biology Details

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

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: 26.87 KDa
Source organism: Trypanosoma brucei brucei
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 3PP 1 x 3PP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 112.36Å b: 97.59Å c: 46.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 not available not available

Quick links

Citations

5 review citations

A role for flexible loops in enzyme catalysis.
Malabanan et al. (2010)
4 more

2 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)
1 more