› 1wob

X-ray diffraction
2.8Å resolution

Structure of a loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed to sulfate

Released:
DOI: 10.2210/pdb1wob/pdb
PDB entry 1wob coloured by chain, front view.
PDB entry 1wob coloured by chain, side view.
PDB entry 1wob coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.
Eaazhisai K, Balaram H, Balaram P, Murthy MR
J Mol Biol 343 671-84 (2004)
PMID: 15465054

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 248 amino acids
Theoretical weight: 27.96 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 SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 50.67Å b: 107.07Å c: 181.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.222
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)
5 other articles

1 mention without citation

Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.
Lopez-Zavala et al. (2016)