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› 1n55

X-ray diffraction
0.83Å resolution

0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate

Released:
DOI: 10.2210/pdb1n55/pdb
Model geometry
Fit model/data
PDB entry 1n55 coloured by chain, front view.
PDB entry 1n55 coloured by chain, side view.
PDB entry 1n55 coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
Kursula I, Wierenga RK
J Biol Chem 278 9544-51 (2003)
PMID: 12522213

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = dihydroxyacetone 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: Escherichia coli
UniProt:
  • Canonical: P48499 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand PGA 1 x PGA
Ligand ACY 2 x ACY
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2
Unit cell:
a: 100.072Å b: 50.58Å c: 58.884Å
α: 90° β: 118.09° γ: 90°
R-values:
R R work R free
0.095 0.095 0.108
Expression system: Escherichia coli

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Citations

7 review citations

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

18 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)
17 more