› 2esd

X-ray diffraction
2.55Å resolution

Crystal Structure of thioacylenzyme intermediate of an Nadp Dependent Aldehyde Dehydrogenase

Released:
DOI: 10.2210/pdb2esd/pdb
PDB entry 2esd coloured by chain, front view.
PDB entry 2esd coloured by chain, side view.
PDB entry 2esd coloured by chain, top view.
Source organism: Streptococcus mutans
Primary publication:
The first crystal structure of a thioacylenzyme intermediate in the ALDH family: new coenzyme conformation and relevance to catalysis.
D'Ambrosio K, Pailot A, Talfournier F, Didierjean C, Benedetti E, Aubry A, Branlant G, Corbier C
Biochemistry 45 2978-86 (2006)
PMID: 16503652

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 475 amino acids
Theoretical weight: 51.22 KDa
Source organism: Streptococcus mutans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59931 (Residues: 1-475; Coverage: 100%)
Gene names: SMU_676, gapN
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
1 bound ligand:
Ligand G3H 4 x G3H
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21212
Unit cell:
a: 142.5Å b: 154.9Å c: 112.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.248
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily.
Marchitti et al. (2008)
5 more

4 mentions without citation

Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation.
Agarwal et al. (2014)
3 more