› 1a7k

X-ray diffraction
2.8Å resolution

GLYCOSOMAL GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN A MONOCLINIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb1a7k/pdb
PDB entry 1a7k coloured by chain, front view.
PDB entry 1a7k coloured by chain, side view.
PDB entry 1a7k coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Crystal structure of Leishmania mexicana glycosomal glyceraldehyde-3-phosphate dehydrogenase in a new crystal form confirms the putative physiological active site structure.
Kim H, Hol WG
J Mol Biol 278 5-11 (1998)
PMID: 9571030

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-173289 (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: 360 amino acids
Theoretical weight: 38.95 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27890 (Residues: 2-361; Coverage: 100%)
Gene name: GAPG
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 67.9Å b: 81Å c: 131.9Å
α: 90° β: 95° γ: 90°
R-values:
R R work R free
0.217 0.217 0.292
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enzymes of carbohydrate metabolism as potential drug targets.
Opperdoes et al. (2001)
12 other articles

6 mentions without citation

Copaifera of the Neotropics: A Review of the Phytochemistry and Pharmacology.
da Trindade et al. (2018)
5 more