1dbv

X-ray diffraction
2.5Å resolution

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (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: 35.88 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 NAD 4 x NAD
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 82.95Å b: 124.68Å c: 82.87Å
α: 90° β: 108.63° γ: 90°
R-values:
R R work R free
0.14 0.14 0.214
Expression system: Escherichia coli