› 1trd

X-ray diffraction
2.5Å resolution

THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM

Released:
DOI: 10.2210/pdb1trd/pdb
PDB entry 1trd coloured by chain, front view.
PDB entry 1trd coloured by chain, side view.
PDB entry 1trd coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism.
Noble ME, Zeelen JP, Wierenga RK
Proteins 16 311-26 (1993)
PMID: 8356028

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

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138175 (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: 26.87 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

1 bound ligand:
Ligand PGH 1 x PGH
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 94.62Å b: 48Å c: 131.31Å
α: 90° β: 100.33° γ: 90°
R-values:
R R work R free
0.147 0.147 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
1 more

14 mentions without citation

Enzyme architecture: on the importance of being in a protein cage.
Richard et al. (2014)
13 more