› 4dbv

X-ray diffraction
2.5Å resolution

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+

Released:
DOI: 10.2210/pdb4dbv/pdb
PDB entry 4dbv coloured by chain, front view.
PDB entry 4dbv coloured by chain, side view.
PDB entry 4dbv coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+.
Didierjean C, Rahuel-Clermont S, Vitoux B, Dideberg O, Branlant G, Aubry A
J Mol Biol 268 739-59 (1997)
PMID: 9175858

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-132434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: O, P, Q, R
Molecule details ›
Chains: O, P, Q, R
Length: 334 amino acids
Theoretical weight: 35.82 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00362 (Residues: 2-335; Coverage: 100%)
Gene name: gap
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 4 x NDP
1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21212
Unit cell:
a: 134.14Å b: 123.95Å c: 96.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.147 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration.
Butterfield et al. (2010)
21 other articles