› 1nq5

X-ray diffraction
2.11Å resolution

Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+

Released:
DOI: 10.2210/pdb1nq5/pdb
PDB entry 1nq5 coloured by chain, front view.
PDB entry 1nq5 coloured by chain, side view.
PDB entry 1nq5 coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Crystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate.
Didierjean C, Corbier C, Fatih M, Favier F, Boschi-Muller S, Branlant G, Aubry A
J Biol Chem 278 12968-76 (2003)
PMID: 12569100

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132433 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: A, C, O, Q
Molecule details ›
Chains: A, C, O, Q
Length: 334 amino acids
Theoretical weight: 35.97 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:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2
Unit cell:
a: 140.48Å b: 87.909Å c: 119.925Å
α: 90° β: 119° γ: 90°
R-values:
R R work R free
0.203 0.198 0.249
Expression system: Escherichia coli

Quick links

Citations

20 citation in other articles

The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation.
Zaffagnini et al. (2007)
19 more

1 mention without citation

Exploring functionally related enzymes using radially distributed properties of active sites around the reacting points of bound ligands.
Ueno et al. (2012)