› 1m6j

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA

Released:
DOI: 10.2210/pdb1m6j/pdb
PDB entry 1m6j coloured by chain, front view.
PDB entry 1m6j coloured by chain, side view.
PDB entry 1m6j coloured by chain, top view.
Source organism: Entamoeba histolytica
Primary publication:
Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica.
Rodríguez-Romero A, Hernández-Santoyo A, del Pozo Yauner L, Kornhauser A, Fernández-Velasco DA
J Mol Biol 322 669-75 (2002)
PMID: 12270704

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-126418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 27.96 KDa
Source organism: Entamoeba histolytica
Expression system: Escherichia coli
UniProt:
  • Canonical: O02611 (Residues: 1-261; Coverage: 100%)
Gene names: EHI_056480, TPI
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21212
Unit cell:
a: 85.729Å b: 119.947Å c: 50.392Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.206
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Therapeutic targets for the treatment of microsporidiosis in humans.
Han et al. (2018)
1 more

7 mentions without citation

Loop motions of triosephosphate isomerase observed with elastic networks.
Kurkcuoglu et al. (2006)
6 more