› 1t10

X-ray diffraction
2.35Å resolution

Phosphoglucose isomerase from Leishmania mexicana in complex with substrate D-fructose-6-phosphate

Released:
DOI: 10.2210/pdb1t10/pdb
PDB entry 1t10 coloured by chain, front view.
PDB entry 1t10 coloured by chain, side view.
PDB entry 1t10 coloured by chain, top view.
Source organism: Leishmania mexicana mexicana
Primary publication:
The crystal structure of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features.
Cordeiro AT, Michels PA, Delboni LF, Thiemann OH
Eur J Biochem 271 2765-72 (2004)
PMID: 15206941

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-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-154901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 67.36 KDa
Source organism: Leishmania mexicana mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: P42861 (Residues: 1-605; Coverage: 100%)
Gene name: PGI
Sequence domains: Phosphoglucose isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand F6P 1 x F6P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P6122
Unit cell:
a: 85.129Å b: 85.129Å c: 350.089Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.22 0.26
Expression system: Escherichia coli

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Citations

16 citation in other articles

Excretory-secretory proteome of larval Schistosoma mansoni and Echinostoma caproni, two parasites of Biomphalaria glabrata.
Guillou et al. (2007)
15 more

8 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)
7 more