› 2y61

X-ray diffraction
0.99Å resolution

Crystal structure of Leishmanial E65Q-TIM complexed with S-Glycidol phosphate

Released:
DOI: 10.2210/pdb2y61/pdb
PDB entry 2y61 coloured by chain, front view.
PDB entry 2y61 coloured by chain, side view.
PDB entry 2y61 coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: the conformational flexibility of the catalytic glutamate in its closed, liganded active site.
Venkatesan R, Alahuhta M, Pihko PM, Wierenga RK
Protein Sci 20 1387-97 (2011)
PMID: 21633986

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 27.21 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P48499 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand 1GP 1 x 1GP
Ligand G3P 1 x G3P
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: C2
Unit cell:
a: 97.14Å b: 52.47Å c: 58.09Å
α: 90° β: 117.85° γ: 90°
R-values:
R R work R free
0.106 not available 0.125
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Antileishmanial phytochemical phenolics: molecular docking to potential protein targets.
Ogungbe et al. (2014)
3 more

3 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)
2 more