› 1k3t

X-ray diffraction
1.95Å resolution

Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi Complexed with Chalepin, a Coumarin Derivative Inhibitor

Released:
DOI: 10.2210/pdb1k3t/pdb
PDB entry 1k3t coloured by chain, front view.
PDB entry 1k3t coloured by chain, side view.
PDB entry 1k3t coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Structure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 A resolution.
Pavão F, Castilho MS, Pupo MT, Dias RL, Correa AG, Fernandes JB, da Silva MF, Mafezoli J, Vieira PC, Oliva G
FEBS Lett 520 13-7 (2002)
PMID: 12044862

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase, glycosomal Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 359 amino acids
Theoretical weight: 39.11 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: P22513 (Residues: 1-359; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 82.08Å b: 84.97Å c: 105.24Å
α: 90° β: 96.32° γ: 90°
R-values:
R R work R free
0.201 0.201 0.28
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Chalepin and Chalepensin: Occurrence, Biosynthesis and Therapeutic Potential.
Nahar et al. (2021)
1 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