› 1amk

X-ray diffraction
1.83Å resolution

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-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: Not provided
UniProt:
  • Canonical: P48499 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 99.09Å b: 52.94Å c: 58.85Å
α: 90° β: 118.13° γ: 90°
R-values:
R R work R free
0.107 0.107 not available
Expression system: Not provided

Quick links

Citations

11 review citations

Rational engineering of enzyme stability.
Eijsink et al. (2004)
10 more

14 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)
13 more