› 4z0s

X-ray diffraction
2.39Å resolution

F96A Mutant of Plasmodium Falciparum Triosephosphate Isomerase

Released:
DOI: 10.2210/pdb4z0s/pdb
PDB entry 4z0s coloured by chain, front view.
PDB entry 4z0s coloured by chain, side view.
PDB entry 4z0s coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme.
Pareek V, Samanta M, Joshi NV, Balaram H, Murthy MR, Balaram P
Chembiochem 17 620-9 (2016)
PMID: 26762569

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

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: 27.92 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 EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 39.42Å b: 76.84Å c: 76.57Å
α: 90° β: 99.44° γ: 90°
R-values:
R R work R free
0.23 0.228 0.271
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.
Olivares-Illana et al. (2017)
1 more