X-ray diffraction
1.72Å resolution

Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase


Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Triosephosphate isomerase, glycosomal Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 250 amino acids
Theoretical weight: 26.82 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
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 BL7-1
Spacegroup: P21
Unit cell:
a: 70.847Å b: 87.9Å c: 74.848Å
α: 90° β: 106.01° γ: 90°
R R work R free
0.189 0.187 0.227
Expression system: Escherichia coli