› 3pvf

X-ray diffraction
1.73Å resolution

Structure of C126S mutant of Plasmodium falciparum triosephosphate isomerase complexed with PGA

Released:
DOI: 10.2210/pdb3pvf/pdb
PDB entry 3pvf coloured by chain, front view.
PDB entry 3pvf coloured by chain, side view.
PDB entry 3pvf coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability.
Samanta M, Banerjee M, Murthy MR, Balaram H, Balaram P
FEBS J 278 1932-43 (2011)
PMID: 21447068

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-170465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 27.98 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 PGA 1 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2
Unit cell:
a: 87.51Å b: 63.1Å c: 53.2Å
α: 90° β: 117.23° γ: 90°
R-values:
R R work R free
0.154 0.152 0.194
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)
9 other articles

1 mention without citation

Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.
Hernández-Santoyo et al. (2012)