› 1m7o

X-ray diffraction
2.4Å resolution

Plasmodium Falciparum Triosephosphate isomerase (PfTIM) compled to substrate analog 3-phosphoglycerate (3PG)

Released:
DOI: 10.2210/pdb1m7o/pdb
PDB entry 1m7o coloured by chain, front view.
PDB entry 1m7o coloured by chain, side view.
PDB entry 1m7o coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
Parthasarathy S, Balaram H, Balaram P, Murthy MR
Acta Crystallogr D Biol Crystallogr 58 1992-2000 (2002)
PMID: 12454456

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-170466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 28 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07412 (Residues: 1-248; Coverage: 100%)
Gene name: TPI
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 3PG 2 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 54.26Å b: 51.345Å c: 90.36Å
α: 90° β: 91.38° γ: 90°
R-values:
R R work R free
0.183 0.183 0.225
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
Aparicio et al. (2003)
5 more

1 mention 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)