› 3iwj

X-ray diffraction
2.15Å resolution

Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)

Released:
DOI: 10.2210/pdb3iwj/pdb
PDB entry 3iwj coloured by chain, front view.
PDB entry 3iwj coloured by chain, side view.
PDB entry 3iwj coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
Tylichová M, Kopecný D, Moréra S, Briozzo P, Lenobel R, Snégaroff J, Sebela M
J Mol Biol 396 870-82 (2010)
PMID: 20026072

Function and Biology Details

Reactions catalysed: 
4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH
4-guanidinobutanal + NAD(+) + H(2)O = 4-guanidinobutanoate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoaldehyde dehydrogenase 2, peroxisomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 503 amino acids
Theoretical weight: 54.55 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93YB2 (Residues: 1-503; Coverage: 100%)
Gene name: AMADH2
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand NA 2 x NA
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 66.25Å b: 86.73Å c: 179.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.234 0.289
Expression system: Escherichia coli

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Citations

1 review citation

Polyamine-Derived Aminoaldehydes and Acrolein: Cytotoxicity, Reactivity and Analysis of the Induced Protein Modifications.
Šebela et al. (2023)
26 other articles

4 mentions without citation

Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate.
Kopečny et al. (2013)
3 more