1m6j

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA

Released:

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (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 name: 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