› 1tpe

X-ray diffraction
2.1Å resolution

COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS

Released:
DOI: 10.2210/pdb1tpe/pdb
PDB entry 1tpe coloured by chain, front view.
PDB entry 1tpe coloured by chain, side view.
PDB entry 1tpe coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK
Protein Sci 3 779-87 (1994)
PMID: 8061607

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-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 26.95 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Not provided
UniProt:
  • 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
Spacegroup: C2
Unit cell:
a: 95.4Å b: 48.2Å c: 67.5Å
α: 90° β: 120° γ: 90°
R-values:
R R work R free
0.155 0.155 not available
Expression system: Not provided

Quick links

Citations

1 review citation

Protein crystallization.
Durbin et al. (1996)
12 other articles

2 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
1 more