2j27

X-ray diffraction
1.15Å resolution

The functional role of the conserved active site proline of triosephosphate isomerase

Released:

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.84 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 45.81Å b: 97.32Å c: 112.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 not available 0.19
Expression system: Escherichia coli BL21