› 1dkw

X-ray diffraction
2.65Å resolution

CRYSTAL STRUCTURE OF TRIOSE-PHOSPHATE ISOMERASE WITH MODIFIED SUBSTRATE BINDING SITE

Released:
DOI: 10.2210/pdb1dkw/pdb
PDB entry 1dkw coloured by chain, front view.
PDB entry 1dkw coloured by chain, side view.
PDB entry 1dkw coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity.
Norledge BV, Lambeir AM, Abagyan RA, Rottmann A, Fernandez AM, Filimonov VV, Peter MG, Wierenga RK
Proteins 42 383-9 (2001)
PMID: 11151009

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 25.79 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P04789 (Residues: 2-250; Coverage: 95%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand TBU 2 x TBU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 46.57Å b: 88.53Å c: 56.22Å
α: 90° β: 97.26° γ: 90°
R-values:
R R work R free
0.186 0.183 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The TIM-barrel fold: a versatile framework for efficient enzymes.
Wierenga RK. (2001)
3 more

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