› 6ooi

X-ray diffraction
2.14Å resolution

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-155742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 256 amino acids
Theoretical weight: 28.46 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P48501 (Residues: 1-253; Coverage: 100%)
Gene name: TPI
Sequence domains: Triosephosphate isomerase

Ligands and Environments

4 bound ligands:
Ligand PGA 8 x PGA
Ligand CL 6 x CL
Ligand NA 8 x NA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002+
Spacegroup: P43
Unit cell:
a: 108.05Å b: 108.05Å c: 182.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Candida albicans and Candida glabrata triosephosphate isomerase - a moonlighting protein that can be exposed on the candidal cell surface and bind to human extracellular matrix proteins.
Satala et al. (2021)
1 more

1 mention without citation

Crystal structures of Triosephosphate Isomerases from Taenia solium and Schistosoma mansoni provide insights for vaccine rationale and drug design against helminth parasites.
Jimenez-Sandoval et al. (2020)