› 5bnk

X-ray diffraction
1.8Å resolution

Crystal structure of T75C mutant of Triosephosphate isomerase from Plasmodium falciparum

Released:
DOI: 10.2210/pdb5bnk/pdb
PDB entry 5bnk coloured by chain, front view.
PDB entry 5bnk coloured by chain, side view.
PDB entry 5bnk coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Probing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme.
Bandyopadhyay D, Murthy MR, Balaram H, Balaram P
FEBS J 282 3863-82 (2015)
PMID: 26206206

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-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

2 bound ligands:
Ligand EDO 2 x EDO
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 39.36Å b: 76.88Å c: 74.48Å
α: 90° β: 97.79° γ: 90°
R-values:
R R work R free
0.209 0.206 0.258
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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)
2 other articles

1 mention without citation

Probing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme.
Bandyopadhyay et al. (2015)